ID   MBHS_ECOLI              Reviewed;         372 AA.
AC   P69739; P19928;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Hydrogenase-1 small chain;
DE            Short=HYD1;
DE            EC=1.12.99.6;
DE   AltName: Full=Membrane-bound hydrogenase 1 small subunit;
DE   AltName: Full=NiFe hydrogenase;
DE   Flags: Precursor;
GN   Name=hyaA; OrderedLocusNames=b0972, JW0954;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 46-50.
RX   PubMed=2180913; DOI=10.1128/jb.172.4.1969-1977.1990;
RA   Menon N.K., Robbins J., Peck H.D. Jr., Chatelus C.Y., Choi E.-S.,
RA   Przybyla A.E.;
RT   "Cloning and sequencing of a putative Escherichia coli [NiFe] hydrogenase-1
RT   operon containing six open reading frames.";
RL   J. Bacteriol. 172:1969-1977(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [5]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [6]
RP   EXPORT VIA THE TAT-SYSTEM.
RX   PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA   Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA   Palmer T., Georgiou G.;
RT   "Export pathway selectivity of Escherichia coli twin arginine translocation
RT   signal peptides.";
RL   J. Biol. Chem. 282:8309-8316(2007).
CC   -!- FUNCTION: This is one of three E.coli hydrogenases synthesized in
CC       response to different physiological conditions. HYD1 is believed to
CC       have a role in hydrogen cycling during fermentative growth.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6;
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P21853};
CC       Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P21853};
CC   -!- COFACTOR:
CC       Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC         Evidence={ECO:0000250|UniProtKB:P21853};
CC       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P21853};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- INTERACTION:
CC       P69739; P0ACD8: hyaB; NbExp=6; IntAct=EBI-9124108, EBI-851493;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type I membrane
CC       protein; Periplasmic side.
CC   -!- PTM: Exported by the Tat system. The position of the signal peptide
CC       cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC       family. {ECO:0000305}.
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DR   EMBL; M34825; AAA23997.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74057.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35737.2; -; Genomic_DNA.
DR   PIR; JV0072; HQECSN.
DR   RefSeq; NP_415491.1; NC_000913.3.
DR   RefSeq; WP_001058323.1; NZ_SSZK01000002.1.
DR   PDB; 3UQY; X-ray; 1.47 A; S/T=46-372.
DR   PDB; 3USC; X-ray; 2.00 A; S/T=46-372.
DR   PDB; 3USE; X-ray; 1.67 A; S/T=46-372.
DR   PDB; 4GD3; X-ray; 3.30 A; Q/R/S/T=46-372.
DR   PDB; 4UE3; X-ray; 1.40 A; S/T=46-372.
DR   PDB; 5A4F; X-ray; 1.25 A; S/T=46-372.
DR   PDB; 5A4I; X-ray; 1.23 A; S/T=46-372.
DR   PDB; 5A4M; X-ray; 1.70 A; S/T=46-311.
DR   PDB; 5ADU; X-ray; 1.10 A; S/T=46-372.
DR   PDB; 5JRD; X-ray; 1.20 A; S/T=46-372.
DR   PDB; 5LMM; X-ray; 1.20 A; S/T=46-372.
DR   PDB; 5LRY; X-ray; 1.40 A; S/T=46-372.
DR   PDB; 6FPI; X-ray; 1.50 A; S/T=46-372.
DR   PDB; 6FPO; X-ray; 1.05 A; S/T=46-372.
DR   PDB; 6FPW; X-ray; 1.35 A; S/T=46-372.
DR   PDB; 6G7R; X-ray; 1.20 A; S/T=46-372.
DR   PDB; 6G94; X-ray; 2.50 A; Q/R/S/T=46-372.
DR   PDB; 6GAL; X-ray; 1.25 A; S/T=46-372.
DR   PDB; 6RP2; X-ray; 1.35 A; S/T=49-372.
DR   PDBsum; 3UQY; -.
DR   PDBsum; 3USC; -.
DR   PDBsum; 3USE; -.
DR   PDBsum; 4GD3; -.
DR   PDBsum; 4UE3; -.
DR   PDBsum; 5A4F; -.
DR   PDBsum; 5A4I; -.
DR   PDBsum; 5A4M; -.
DR   PDBsum; 5ADU; -.
DR   PDBsum; 5JRD; -.
DR   PDBsum; 5LMM; -.
DR   PDBsum; 5LRY; -.
DR   PDBsum; 6FPI; -.
DR   PDBsum; 6FPO; -.
DR   PDBsum; 6FPW; -.
DR   PDBsum; 6G7R; -.
DR   PDBsum; 6G94; -.
DR   PDBsum; 6GAL; -.
DR   PDBsum; 6RP2; -.
DR   AlphaFoldDB; P69739; -.
DR   SMR; P69739; -.
DR   BioGRID; 4261801; 75.
DR   BioGRID; 849953; 2.
DR   ComplexPortal; CPX-281; Hydrogenase-1 complex.
DR   DIP; DIP-47848N; -.
DR   IntAct; P69739; 5.
DR   STRING; 511145.b0972; -.
DR   jPOST; P69739; -.
DR   PaxDb; 511145-b0972; -.
DR   EnsemblBacteria; AAC74057; AAC74057; b0972.
DR   GeneID; 66670752; -.
DR   GeneID; 945579; -.
DR   KEGG; ecj:JW0954; -.
DR   KEGG; eco:b0972; -.
DR   PATRIC; fig|1411691.4.peg.1302; -.
DR   EchoBASE; EB0463; -.
DR   eggNOG; COG1740; Bacteria.
DR   HOGENOM; CLU_046107_0_0_6; -.
DR   InParanoid; P69739; -.
DR   OMA; VPGCPIQ; -.
DR   OrthoDB; 9766729at2; -.
DR   PhylomeDB; P69739; -.
DR   BioCyc; EcoCyc:HYAA-MONOMER; -.
DR   BioCyc; MetaCyc:HYAA-MONOMER; -.
DR   BRENDA; 1.12.99.6; 2026.
DR   PHI-base; PHI:11000; -.
DR   PRO; PR:P69739; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0044569; C:[Ni-Fe] hydrogenase complex; IDA:EcoCyc.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR   GO; GO:0098567; C:periplasmic side of plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IC:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR   GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR   GO; GO:0009267; P:cellular response to starvation; IDA:ComplexPortal.
DR   GO; GO:0006113; P:fermentation; IDA:ComplexPortal.
DR   GO; GO:1902421; P:hydrogen metabolic process; IC:EcoCyc.
DR   Gene3D; 4.10.480.10; Cytochrome-c3 hydrogenase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.700; NADH:ubiquinone oxidoreductase-like, 20kDa subunit; 1.
DR   InterPro; IPR027394; Cytochrome-c3_hydrogenase_C.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR037148; NiFe-Hase_small_C_sf.
DR   InterPro; IPR037024; NiFe_Hase_small_N_sf.
DR   InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR00391; hydA; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR   PANTHER; PTHR30013:SF6; HYDROGENASE-1 SMALL CHAIN; 1.
DR   PANTHER; PTHR30013; NIFE / NIFESE HYDROGENASE SMALL SUBUNIT FAMILY MEMBER; 1.
DR   Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR   PRINTS; PR00614; NIHGNASESMLL.
DR   SUPFAM; SSF56770; HydA/Nqo6-like; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 3Fe-4S; 4Fe-4S; Cell inner membrane; Cell membrane;
KW   Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..45
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:2180913"
FT   CHAIN           46..372
FT                   /note="Hydrogenase-1 small chain"
FT                   /id="PRO_0000013427"
FT   TOPO_DOM        46..325
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        349..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          347..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         160
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         194
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         232
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         235
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         260
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         266
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         275
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         294
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   BINDING         297
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000250|UniProtKB:P21853"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           64..70
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   TURN            73..76
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           77..83
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   TURN            91..93
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           98..111
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   TURN            112..115
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           140..150
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          151..157
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           158..162
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           179..181
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          188..191
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           198..211
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           231..233
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           238..243
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           268..270
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   TURN            281..284
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   TURN            287..291
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           302..304
FT                   /evidence="ECO:0007829|PDB:6FPO"
FT   HELIX           320..339
FT                   /evidence="ECO:0007829|PDB:6G94"
FT   STRAND          346..349
FT                   /evidence="ECO:0007829|PDB:4GD3"
SQ   SEQUENCE   372 AA;  40681 MW;  4AD3ECB4220D2826 CRC64;
     MNNEETFYQA MRRQGVTRRS FLKYCSLAAT SLGLGAGMAP KIAWALENKP RIPVVWIHGL
     ECTCCTESFI RSAHPLAKDV ILSLISLDYD DTLMAAAGTQ AEEVFEDIIT QYNGKYILAV
     EGNPPLGEQG MFCISSGRPF IEKLKRAAAG ASAIIAWGTC ASWGCVQAAR PNPTQATPID
     KVITDKPIIK VPGCPPIPDV MSAIITYMVT FDRLPDVDRM GRPLMFYGQR IHDKCYRRAH
     FDAGEFVQSW DDDAARKGYC LYKMGCKGPT TYNACSSTRW NDGVSFPIQS GHGCLGCAEN
     GFWDRGSFYS RVVDIPQMGT HSTADTVGLT ALGVVAAAVG VHAVASAVDQ RRRHNQQPTE
     TEHQPGNEDK QA
//