HYBA_ECOLI
ID HYBA_ECOLI Reviewed; 328 AA.
AC P0AAJ8; P37179; Q2M9J9;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Hydrogenase-2 operon protein HybA;
DE Flags: Precursor;
GN Name=hybA; OrderedLocusNames=b2996, JW2964;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / TG1;
RX PubMed=8021226; DOI=10.1128/jb.176.14.4416-4423.1994;
RA Menon N.K., Chatelus C.Y., Dervartanian M., Wendt J.C., Shanmugam K.T.,
RA Peck H.D. Jr., Przybyla A.E.;
RT "Cloning, sequencing, and mutational analysis of the hyb operon encoding
RT Escherichia coli hydrogenase 2.";
RL J. Bacteriol. 176:4416-4423(1994).
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 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: Participates in the periplasmic electron-transferring
CC activity of hydrogenase 2 during its catalytic turnover.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven. Can also be exported by
CC the Sec system.
CC -!- CAUTION: Was originally thought to be the small subunit of hydrogenase
CC 2. {ECO:0000305|PubMed:8021226}.
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DR EMBL; U09177; AAA21589.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69163.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76032.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77057.1; -; Genomic_DNA.
DR PIR; B65086; B65086.
DR RefSeq; NP_417470.1; NC_000913.3.
DR RefSeq; WP_001081870.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AAJ8; -.
DR BioGRID; 4263111; 20.
DR BioGRID; 849242; 2.
DR ComplexPortal; CPX-282; Hydrogenase-2 complex.
DR IntAct; P0AAJ8; 6.
DR STRING; 511145.b2996; -.
DR jPOST; P0AAJ8; -.
DR PaxDb; P0AAJ8; -.
DR PRIDE; P0AAJ8; -.
DR EnsemblBacteria; AAC76032; AAC76032; b2996.
DR EnsemblBacteria; BAE77057; BAE77057; BAE77057.
DR GeneID; 66673106; -.
DR GeneID; 944842; -.
DR KEGG; ecj:JW2964; -.
DR KEGG; eco:b2996; -.
DR PATRIC; fig|1411691.4.peg.3733; -.
DR EchoBASE; EB1747; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_0_0_6; -.
DR InParanoid; P0AAJ8; -.
DR OMA; PKYDYDN; -.
DR PhylomeDB; P0AAJ8; -.
DR BioCyc; EcoCyc:HYBA-MON; -.
DR BioCyc; MetaCyc:HYBA-MON; -.
DR PRO; PR:P0AAJ8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0044569; C:[Ni-Fe] hydrogenase complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0019645; P:anaerobic electron transport chain; IDA:ComplexPortal.
DR GO; GO:0019588; P:anaerobic glycerol catabolic process; IDA:EcoCyc.
DR GO; GO:0009061; P:anaerobic respiration; IDA:ComplexPortal.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF13247; Fer4_11; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255"
FT CHAIN 28..328
FT /note="Hydrogenase-2 operon protein HybA"
FT /id="PRO_0000042273"
FT DOMAIN 38..68
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 103..134
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 136..165
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 47
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 36003 MW; 77203A0F50F61662 CRC64;
MNRRNFIKAA SCGALLTGAL PSVSHAAAEN RPPIPGSLGM LYDSTLCVGC QACVTKCQDI
NFPERNPQGE QTWSNNDKLS PYTNNIIQVW TSGTGVNKDQ EENGYAYIKK QCMHCVDPNC
VSVCPVSALK KDPKTGIVHY DKDVCTGCRY CMVACPYNVP KYDYNNPFGA LHKCELCNQK
GVERLDKGGL PGCVEVCPAG AVIFGTREEL MAEAKKRLAL KPGSEYHYPR QTLKSGDTYL
HTVPKYYPHL YGEKEGGGTQ VLVLTGVPYE NLDLPKLDDL STGARSENIQ HTLYKGMMLP
LAVLAGLTVL VRRNTKNDHH DGGDDHES
