MBHS_ECOLI
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 03-AUG-2022, entry version 132.
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; Proteobacteria; 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=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250};
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; 6FPI; X-ray; 1.50 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; 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; 6FPI; -.
DR PDBsum; 6FPW; -.
DR PDBsum; 6G7R; -.
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; P69739; -.
DR PRIDE; P69739; -.
DR EnsemblBacteria; AAC74057; AAC74057; b0972.
DR EnsemblBacteria; BAA35737; BAA35737; BAA35737.
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; RSFNAHN; -.
DR PhylomeDB; P69739; -.
DR BioCyc; EcoCyc:HYAA-MON; -.
DR BioCyc; MetaCyc:HYAA-MON; -.
DR BRENDA; 1.12.99.6; 2026.
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:0016021; C:integral component of membrane; ISM:EcoCyc.
DR GO; GO:0031237; C:intrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
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; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.700; -; 1.
DR Gene3D; 4.10.480.10; -; 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 PANTHER; PTHR30013; PTHR30013; 1.
DR Pfam; PF14720; NiFe_hyd_SSU_C; 1.
DR Pfam; PF01058; Oxidored_q6; 1.
DR PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR TIGRFAMs; TIGR00391; hydA; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 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"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 297
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:5ADU"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:5ADU"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 98..111
FT /evidence="ECO:0007829|PDB:5ADU"
FT TURN 112..115
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5ADU"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5ADU"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:5ADU"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:5ADU"
FT TURN 287..291
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5ADU"
FT HELIX 320..338
FT /evidence="ECO:0007829|PDB:4GD3"
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
