MBHT_ECOLI
ID MBHT_ECOLI Reviewed; 372 AA.
AC P69741; Q2M9J8; Q46847;
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-2 small chain;
DE Short=HYD2;
DE EC=1.12.99.6;
DE AltName: Full=Membrane-bound hydrogenase 2 small subunit;
DE AltName: Full=NiFe hydrogenase;
DE Flags: Precursor;
GN Name=hybO; Synonyms=yghV; OrderedLocusNames=b2997, JW2965;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 38-47 AND 218-234, CHARACTERIZATION, AND EXPORT VIA THE
RP TAT-SYSTEM.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9738917; DOI=10.1046/j.1432-1327.1998.2550746.x;
RA Sargent F., Ballantine S.P., Rugman P.A., Palmer T., Boxer D.H.;
RT "Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small
RT subunit -- identification of a soluble precursor of the small subunit in a
RT hypB mutant.";
RL Eur. J. Biochem. 255:746-754(1998).
RN [4]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-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. HYD2 is involved in
CC hydrogen uptake.
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 P69741; P0AAN1: hybE; NbExp=6; IntAct=EBI-552619, EBI-552588;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Periplasmic side. Periplasm.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has been experimentally proven. Can also be exported by the
CC Sec system.
CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small subunit
CC family. {ECO:0000305}.
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DR EMBL; U28377; AAA69164.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76033.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77058.1; -; Genomic_DNA.
DR PIR; C65086; C65086.
DR RefSeq; NP_417471.1; NC_000913.3.
DR RefSeq; WP_000145410.1; NZ_STEB01000001.1.
DR PDB; 6EHQ; X-ray; 2.20 A; S/T=38-330.
DR PDB; 6EHS; X-ray; 1.50 A; S/T=38-330.
DR PDB; 6EN9; X-ray; 1.50 A; S/T=39-331.
DR PDB; 6G7M; X-ray; 1.71 A; S/T=38-333.
DR PDB; 6GAM; X-ray; 1.40 A; S/T=38-330.
DR PDB; 6GAN; X-ray; 1.60 A; S/T=38-330.
DR PDB; 6SYO; X-ray; 1.25 A; SSS/TTT=39-331.
DR PDB; 6SYX; X-ray; 1.30 A; SSS/TTT=39-330.
DR PDB; 6SZD; X-ray; 1.50 A; SSS/TTT=39-330.
DR PDB; 6SZK; X-ray; 1.20 A; SSS/TTT=39-330.
DR PDB; 7NEM; X-ray; 1.35 A; S/T=39-330.
DR PDBsum; 6EHQ; -.
DR PDBsum; 6EHS; -.
DR PDBsum; 6EN9; -.
DR PDBsum; 6G7M; -.
DR PDBsum; 6GAM; -.
DR PDBsum; 6GAN; -.
DR PDBsum; 6SYO; -.
DR PDBsum; 6SYX; -.
DR PDBsum; 6SZD; -.
DR PDBsum; 6SZK; -.
DR PDBsum; 7NEM; -.
DR AlphaFoldDB; P69741; -.
DR SMR; P69741; -.
DR BioGRID; 4261299; 260.
DR BioGRID; 850267; 10.
DR ComplexPortal; CPX-282; Hydrogenase-2 complex.
DR DIP; DIP-36024N; -.
DR IntAct; P69741; 17.
DR MINT; P69741; -.
DR STRING; 511145.b2997; -.
DR jPOST; P69741; -.
DR PaxDb; P69741; -.
DR PRIDE; P69741; -.
DR EnsemblBacteria; AAC76033; AAC76033; b2997.
DR EnsemblBacteria; BAE77058; BAE77058; BAE77058.
DR GeneID; 66673105; -.
DR GeneID; 945902; -.
DR KEGG; ecj:JW2965; -.
DR KEGG; eco:b2997; -.
DR PATRIC; fig|1411691.4.peg.3732; -.
DR EchoBASE; EB2828; -.
DR eggNOG; COG1740; Bacteria.
DR HOGENOM; CLU_046107_0_1_6; -.
DR InParanoid; P69741; -.
DR OMA; VPGCPIQ; -.
DR PhylomeDB; P69741; -.
DR BioCyc; EcoCyc:MON0-145; -.
DR BioCyc; MetaCyc:MON0-145; -.
DR PRO; PR:P69741; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0044569; C:[Ni-Fe] hydrogenase complex; IBA:GO_Central.
DR GO; GO:0031236; C:extrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; ISM: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 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 membrane; Direct protein sequencing;
KW Iron; Iron-sulfur; Membrane; Metal-binding; Oxidoreductase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..37
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:9738917"
FT CHAIN 38..372
FT /note="Hydrogenase-2 small chain"
FT /id="PRO_0000013430"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
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 257
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000250"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 156..160
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:6GAM"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:6GAM"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:6GAM"
FT TURN 298..303
FT /evidence="ECO:0007829|PDB:6GAM"
SQ SEQUENCE 372 AA; 39652 MW; C5821096BBAF9C66 CRC64;
MTGDNTLIHS HGINRRDFMK LCAALAATMG LSSKAAAEMA ESVTNPQRPP VIWIGAQECT
GCTESLLRAT HPTVENLVLE TISLEYHEVL SAAFGHQVEE NKHNALEKYK GQYVLVVDGS
IPLKDNGIYC MVAGEPIVDH IRKAAEGAAA IIAIGSCSAW GGVAAAGVNP TGAVSLQEVL
PGKTVINIPG CPPNPHNFLA TVAHIITYGK PPKLDDKNRP TFAYGRLIHE HCERRPHFDA
GRFAKEFGDE GHREGWCLYH LGCKGPETYG NCSTLQFCDV GGVWPVAIGH PCYGCNEEGI
GFHKGIHQLA NVENQTPRSQ KPDVNAKEGG NVSAGAIGLL GGVVGLVAGV SVMAVRELGR
QQKKDNADSR GE
