Hydrogenase-2 small chain precursor - Escherichia coli O157:H7

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P69743 (MBHT_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Hydrogenase-2 small chain
Short name=HYD2
EC=1.12.99.6

Alternative name(s):
Membrane-bound hydrogenase 2 small subunit
NiFe hydrogenase

Gene names

Name:	hybO
Ordered Locus Names:	Z4351, ECs3882

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	372 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (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. Binds 2 4Fe-4S clusters By similarity.
Subunit structure	Heterodimer of a large and a small subunit.
Subcellular location	Cell membrane; Peripheral membrane protein; Periplasmic side. Periplasm.
Post-translational modification	Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.
Sequence similarities	Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane Periplasm
Domain	Signal
Ligand	3Fe-4S 4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Cellular component	ferredoxin hydrogenase complex Inferred from electronic annotation. Source: InterPro periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Inferred from electronic annotation. Source: InterPro ferredoxin hydrogenase activity Inferred from electronic annotation. Source: InterPro hydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 37

Tat-type signal Potential

Chain

38 – 372

335

Hydrogenase-2 small chain

PRO_0000013432

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

157

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

191

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

229

Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity

Metal binding

232

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

257

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

263

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

272

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

292

Iron-sulfur 3 (3Fe-4S) By similarity

Metal binding

295

Iron-sulfur 3 (3Fe-4S) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P69743 [UniParc].

Last modified April 26, 2005. Version 1.
Checksum: C5821096BBAF9C66
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FASTA

372

39,652

        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

« Hide

References

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG58134.1. BA000007 Genomic DNA. Translation: BAB37305.1.
PIR	B85959. B91114.
RefSeq	NP_289575.1. NC_002655.2. NP_311909.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P69743.
SMR	P69743. Positions 46-310.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000024891; EBESCP00000023784; EBESCG00000023945. EBESCT00000060407; EBESCP00000058235; EBESCG00000059454.
GeneID	916289. 958478.
GenomeReviews	Gene locus Z4351 in contig AE005174_GR. Gene locus ECs3882 in contig BA000007_GR.
KEGG	ece:Z4351. ecs:ECs3882.
PATRIC	18357255. VBIEscCol44059_3805.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000010145.
HOGENOM	HBG575615.
OMA	RLIHENC.
ProtClustDB	PRK10468.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS3882-MONOMER.
Family and domain databases
InterPro	IPR006137. NADH_UbQ_OxRdtase-like_20kDa. IPR001821. NiFe_hydrogenase_ssu. IPR006311. TAT_signal. IPR019546. TAT_signal_bac_arc. [Graphical view]
Gene3D	G3DSA:3.40.50.700. G3DSA:3.40.50.700. 1 hit.
KO	K06282.
Pfam	PF01058. Oxidored_q6. 1 hit. [Graphical view]
PIRSF	PIRSF000310. NiFe_hyd_ssu. 1 hit.
PRINTS	PR00614. NIHGNASESMLL.
TIGRFAMs	TIGR00391. HydA. 1 hit. TIGR01409. TAT_signal_seq. 1 hit.
PROSITE	PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MBHT_ECO57

Accession

Primary (citable) accession number: P69743
Secondary accession number(s): Q46847

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents