[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / MG1655 / ATCC 47076; DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan] Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.; "The complete genome sequence of Escherichia coli K-12."; Science 277:1453-1474(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan] Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."; Mol. Syst. Biol. 2:E1-E5(2006).
[3]	PROTEIN SEQUENCE OF 38-47 AND 218-234, CHARACTERIZATION, AND EXPORT VIA THE TAT-SYSTEM. STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; PubMed=9738917 [NCBI, ExPASy, EBI, Israel, Japan] Sargent F., Ballantine S.P., Rugman P.A., Palmer T., Boxer D.H.; "Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit -- identification of a soluble precursor of the small subunit in a hypB mutant."; Eur. J. Biochem. 255:746-754(1998).

Comments

FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake.
CATALYTIC ACTIVITY: H₂ + A = AH₂.
COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
COFACTOR: Binds 2 4Fe-4S clusters (By similarity).
SUBUNIT: Heterodimer of a large and a small subunit.
INTERACTION:
P0AAN1:hybE; NbExp=2; IntAct=EBI-552619, EBI-552588;
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Periplasmic side.
PTM: Exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U28377; AAA69164.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76033.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77058.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

C65086; C65086.

RefSeq

AP_003552.1; -.
NP_417471.1; -.

3D structure databases

HSSP

P18187; 1FRF. [HSSP ENTRY / PDB]

ModBase

P69741.

Protein-protein interaction databases

IntAct

P69741; -.

Enzyme and pathway databases

BioCyc

EcoCyc:MON0-145; -.
MetaCyc:MON0-145; -.

Organism-specific databases

EchoBASE

EB2828; -.

EcoGene

EG13006; hybO.

Ontologies

GO:0009375;	Cellular component: ferredoxin hydrogenase complex (inferred from electronic annotation from InterPro).
GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0051538;	Molecular function: 3 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051539;	Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008901;	Molecular function: ferredoxin hydrogenase activity (inferred from electronic annotation from InterPro).
GO:0033748;	Molecular function: hydrogenase (acceptor) activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008137;	Molecular function: NADH dehydrogenase (ubiquinone) activity (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006120;	Biological process: mitochondrial electron transport, NADH to ubiquinone (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001821; NiFe_hyd_ssu.
IPR013634; NiFe_hyd_ssu_N.
IPR006137; OxRdtase_q6.
IPR006311; Tat.
Graphical view of domain structure.

Pfam

PF08425; NiFe_dehyd_N; 1.
PF01058; Oxidored_q6; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000310; NiFe_hyd_ssu; 1.

PRINTS

PR00614; NIHGNASESMLL.

TIGRFAMs

TIGR00391; hydA; 1.
TIGR01409; TAT_signal_seq; 1.

PROSITE

PS51318; TAT; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P69741.

Genome annotation databases

GeneID

945902; -.

GenomeReviews

U00096_GR; b2997.
AP009048_GR; JW2965.

KEGG

ecj:JW2965; -.
eco:b2997; -.

Phylogenomic databases

HOGENOM

P69741; -.

Genome annotation databases

CMR

P69741; b2997.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3Fe-4S; 4Fe-4S; Cell membrane; Complete proteome; Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Periplasm; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 37`	`37`	`Tat-type signal.`
`CHAIN`	`38 372`	`335`	`Hydrogenase-2 small chain.`	`PRO_0000013430`
`METAL`	`59 59`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`62 62`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`157 157`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`191 191`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`229 229`		`Iron-sulfur 2 (4Fe-4S); via pros nitrogen (By similarity).`
`METAL`	`232 232`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`257 257`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`263 263`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`272 272`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`292 292`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`295 295`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 39652 Da [This is the MW of the unprocessed precursor]

CRC64: C5821096BBAF9C66 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTGDNTLIHS HGINRRDFMK LCAALAATMG LSSKAAAEMA ESVTNPQRPP VIWIGAQECT 

        70         80         90        100        110        120 
GCTESLLRAT HPTVENLVLE TISLEYHEVL SAAFGHQVEE NKHNALEKYK GQYVLVVDGS 

       130        140        150        160        170        180 
IPLKDNGIYC MVAGEPIVDH IRKAAEGAAA IIAIGSCSAW GGVAAAGVNP TGAVSLQEVL 

       190        200        210        220        230        240 
PGKTVINIPG CPPNPHNFLA TVAHIITYGK PPKLDDKNRP TFAYGRLIHE HCERRPHFDA 

       250        260        270        280        290        300 
GRFAKEFGDE GHREGWCLYH LGCKGPETYG NCSTLQFCDV GGVWPVAIGH PCYGCNEEGI 

       310        320        330        340        350        360 
GFHKGIHQLA NVENQTPRSQ KPDVNAKEGG NVSAGAIGLL GGVVGLVAGV SVMAVRELGR 

       370 
QQKKDNADSR GE

P69741 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools