HYFB_ECOLI
ID HYFB_ECOLI Reviewed; 672 AA.
AC P23482;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Hydrogenase-4 component B;
DE EC=1.-.-.-;
GN Name=hyfB {ECO:0000303|PubMed:9387241}; Synonyms=yffF;
GN OrderedLocusNames=b2482, JW2467;
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 POSSIBLE FUNCTION.
RC STRAIN=K12;
RX PubMed=9387241; DOI=10.1099/00221287-143-11-3633;
RA Andrews S.C., Berks B.C., McClay J., Ambler A., Quail M.A., Golby P.,
RA Guest J.R.;
RT "A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-
RT translocating formate hydrogenlyase system.";
RL Microbiology 143:3633-3647(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RC STRAIN=K12;
RX PubMed=2016588; DOI=10.1099/00221287-137-2-361;
RA Andrews S.C., Harrison P.M., Guest J.R.;
RT "A molecular analysis of the 53.3 minute region of the Escherichia coli
RT linkage map.";
RL J. Gen. Microbiol. 137:361-367(1991).
RN [6]
RP INDUCTION, OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12426353; DOI=10.1128/jb.184.23.6642-6653.2002;
RA Skibinski D.A., Golby P., Chang Y.S., Sargent F., Hoffman R., Harper R.,
RA Guest J.R., Attwood M.M., Berks B.C., Andrews S.C.;
RT "Regulation of the hydrogenase-4 operon of Escherichia coli by the
RT sigma(54)-dependent transcriptional activators FhlA and HyfR.";
RL J. Bacteriol. 184:6642-6653(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND 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).
CC -!- FUNCTION: Possible component of hydrogenase 4.
CC {ECO:0000305|PubMed:9387241}.
CC -!- INTERACTION:
CC P23482; P37052: ychJ; NbExp=2; IntAct=EBI-554793, EBI-560596;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305}.
CC -!- INDUCTION: Most efficiently induced by formate during post-exponential
CC growth at low external pH (pH 6.5) in the absence of respiratory
CC electron acceptors O(2+), NO(3-) or trimethylamine-N-oxide, i.e. under
CC anaerobic control. Transcription is activated by FhlA and HyfR,
CC inhibited by HycA, part of the sigma-54 (rpoN) regulon. Second member
CC of a 10 gene operon (hyfABCDEFGHIJ); it is not clear if the 2 following
CC genes (hydR-focB) are also in the operon.
CC {ECO:0000269|PubMed:12426353}.
CC -!- DISRUPTION PHENOTYPE: Deletion of most of the operon (hyfBCDEFGHIJR)
CC has no visible effect under fermentative growth conditions at pH 6.5 or
CC 7.5, during aerobic or anaerobic glucose-limited growth at pH 6.5, or
CC when combined with hyc mutations. {ECO:0000269|PubMed:12426353}.
CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR EMBL; M63654; AAB88564.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75535.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16360.1; -; Genomic_DNA.
DR PIR; A65024; A65024.
DR RefSeq; NP_416977.1; NC_000913.3.
DR RefSeq; WP_000339455.1; NZ_LN832404.1.
DR AlphaFoldDB; P23482; -.
DR SMR; P23482; -.
DR BioGRID; 4259196; 9.
DR ComplexPortal; CPX-6028; Formate hydrogenlyase-H/Hydrogenase-4 complex.
DR DIP; DIP-9984N; -.
DR IntAct; P23482; 3.
DR STRING; 511145.b2482; -.
DR TCDB; 3.D.1.9.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P23482; -.
DR PRIDE; P23482; -.
DR EnsemblBacteria; AAC75535; AAC75535; b2482.
DR EnsemblBacteria; BAA16360; BAA16360; BAA16360.
DR GeneID; 946961; -.
DR KEGG; ecj:JW2467; -.
DR KEGG; eco:b2482; -.
DR PATRIC; fig|1411691.4.peg.4257; -.
DR EchoBASE; EB1259; -.
DR eggNOG; COG0651; Bacteria.
DR HOGENOM; CLU_007100_8_1_6; -.
DR InParanoid; P23482; -.
DR OMA; AMCFVKV; -.
DR PhylomeDB; P23482; -.
DR BioCyc; EcoCyc:MON0-153; -.
DR PRO; PR:P23482; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009326; C:formate dehydrogenase complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0019645; P:anaerobic electron transport chain; IC:ComplexPortal.
DR GO; GO:0009061; P:anaerobic respiration; IC:ComplexPortal.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR GO; GO:0015944; P:formate oxidation; IC:ComplexPortal.
DR GO; GO:0006007; P:glucose catabolic process; IC:ComplexPortal.
DR InterPro; IPR003918; NADH_UbQ_OxRdtase.
DR InterPro; IPR001750; ND/Mrp_mem.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR PRINTS; PR01437; NUOXDRDTASE4.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..672
FT /note="Hydrogenase-4 component B"
FT /id="PRO_0000118226"
FT TOPO_DOM 1..5
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..79
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..242
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..311
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..384
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..474
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..531
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 672 AA; 72583 MW; 3CA8C2BD25E54B1B CRC64;
MDALQLLTWS LILYLFASLA SLFLLGLDRL AIKLSGITSL VGGVIGIISG ITQLHAGVTL
VARFAPPFEF ADLTLRMDSL SAFMVLVISL LVVVCSLYSL TYMREYEGKG AAAMGFFMNI
FIASMVALLV MDNAFWFIVL FEMMSLSSWF LVIARQDKTS INAGMLYFFI AHAGSVLIMI
AFLLMGRESG SLDFASFRTL SLSPGLASAV FLLAFFGFGA KAGMMPLHSW LPRAHPAAPS
HASALMSGVM VKIGIFGILK VAMDLLAQTG LPLWWGILVM AIGAISALLG VLYALAEQDI
KRLLAWSTVE NVGIILLAVG VAMVGLSLHD PLLTVVGLLG ALFHLLNHAL FKGLLFLGAG
AIISRLHTHD MEKMGALAKR MPWTAAACLI GCLAISAIPP LNGFISEWYT WQSLFSLSRV
EAVALQLAGP IAMVMLAVTG GLAVMCFVKM YGITFCGAPR STHAEEAQEV PNTMIVAMLL
LAALCVLIAL SASWLAPKIM HIAHAFTNTP PATVASGIAL VPGTFHTQVT PSLLLLLLLA
MPLLPGLYWL WCRSRRAAFR RTGDAWACGY GWENAMAPSG NGVMQPLRVV FSALFRLRQQ
LDPTLRLNKG LAHVTARAQS TEPFWDERVI RPIVSATQRL AKEIQHLQSG DFRLYCLYVV
AALVVLLIAI AV
