NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=301 / Serotype 2a;
DOI=10.1093/nar/gkf566; PubMed=12384590 [NCBI, ExPASy, EBI, Israel, Japan]
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157.";
Nucleic Acids Res. 30:4432-4441(2002).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700930 / 2457T / Serotype 2a;
DOI=10.1128/IAI.71.5.2775-2786.2003; PubMed=12704152 [NCBI, ExPASy, EBI, Israel, Japan]
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T.";
Infect. Immun. 71:2775-2786(2003).

Comments

FUNCTION: This is one of three S.flexneri hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth (By similarity).
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 (By similarity).
SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane protein (By similarity).
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not 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

AE005674; AAN42601.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014073; AAP16487.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_706894.2; -.
NP_836681.1; -.

3D structure databases

HSSP

P18187; 1FRF. [HSSP ENTRY / PDB]

ModBase

Q83RW9.

Enzyme and pathway databases

BioCyc

SFLE198214:AAN42601.1-MON; -.

Ontologies

GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0033748;	Molecular function: hydrogenase (acceptor) activity (inferred from electronic annotation from EC).
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).

BLOCKS

Q83RW9.

Genome annotation databases

GeneID

1023950; -.
1077442; -.

GenomeReviews

AE014073_GR; S1040.
AE005674_GR; SF0973.

KEGG

sfl:SF0973; -.
sfx:S1040; -.

Phylogenomic databases

HOGENOM

Q83RW9; -.

Genome annotation databases

CMR

Q83RW9; SF0973.

Other

ProtoNet

Q83RW9.

UniRef

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

Keywords

3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome; Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Periplasm; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 45`	`45`	`Tat-type signal (Potential).`
`CHAIN`	`46 372`	`327`	`Hydrogenase-1 small chain.`	`PRO_0000013429`
`TOPO_DOM`	`46 325`	`280`	`Periplasmic (Potential).`
`TRANSMEM`	`326 346`	`21`	`Potential.`
`TOPO_DOM`	`347 372`	`26`	`Cytoplasmic (Potential).`
`METAL`	`62 62`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`65 65`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`160 160`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`194 194`		`Iron-sulfur 1 (4Fe-4S) (By similarity).`
`METAL`	`232 232`		`Iron-sulfur 2 (4Fe-4S) (via pros nitrogen) (By similarity).`
`METAL`	`235 235`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`260 260`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`266 266`		`Iron-sulfur 2 (4Fe-4S) (By similarity).`
`METAL`	`275 275`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`294 294`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`METAL`	`297 297`		`Iron-sulfur 3 (3Fe-4S) (By similarity).`
`CONFLICT`	`347 347`		`S -> A (in Ref. 2; AAP16487).`

Sequence information

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

Molecular weight: 40697 Da [This is the MW of the unprocessed precursor]

CRC64: 4AC0CD86220D2826 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNNEETFYQA MRRQGVTRRS FLKYCSLAAT SLGLGAGMAP KIAWALENKP RIPVVWIHGL 

        70         80         90        100        110        120 
ECTCCTESFI RSAHPLAKDV ILSLISLDYD DTLMAAAGTQ AEEVFEDIIT QYNGKYILAV 

       130        140        150        160        170        180 
EGNPPLGEQG MFCISSGRPF IEKLKRAAAG ASAIIAWGTC ASWGCVQAAR PNPTQATPID 

       190        200        210        220        230        240 
KVITDKPIIK VPGCPPIPDV MSAIITYMVT FDRLPDVDRM GRPLMFYGQR IHDKCYRRAH 

       250        260        270        280        290        300 
FDAGEFVQSW DDDAARKGYC LYKMGCKGPT TYNACSSTRW NDGVSFPIQS GHGCLGCAEN 

       310        320        330        340        350        360 
GFWDRGSFYS RVVDIPQMGT HSTADTVGLT ALGVVAAAVG VHAVASSVDQ RRRHNQQPTE 

       370 
TEHQPGNEDK QA

Q83RW9 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