NAPB_ECOLI
ID NAPB_ECOLI Reviewed; 149 AA.
AC P0ABL3; P33933; P76453; Q2MAP0;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB;
DE Flags: Precursor;
GN Name=napB; Synonyms=yejY; OrderedLocusNames=b2203, JW5367;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
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 PROTEIN SEQUENCE OF 28-34, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP PTM.
RC STRAIN=K12;
RX PubMed=10234835; DOI=10.1111/j.1574-6968.1999.tb13564.x;
RA Thomas G., Potter L., Cole J.A.;
RT "The periplasmic nitrate reductase from Escherichia coli: a heterodimeric
RT molybdoprotein with a double-arginine signal sequence and an unusual leader
RT peptide cleavage site.";
RL FEMS Microbiol. Lett. 174:167-171(1999).
RN [5]
RP CHARACTERIZATION AS A CYTOCHROME C.
RX PubMed=8039676; DOI=10.1111/j.1574-6968.1994.tb06872.x;
RA Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., Pommier J.,
RA Mejean V., Cole J.A.;
RT "A reassessment of the range of c-type cytochromes synthesized by
RT Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 119:89-94(1994).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, PTM, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=10548535; DOI=10.1042/bj3440069;
RA Potter L.C., Cole J.A.;
RT "Essential roles for the products of the napABCD genes, but not napFGH, in
RT periplasmic nitrate reduction by Escherichia coli K-12.";
RL Biochem. J. 344:69-76(1999).
RN [7]
RP FUNCTION, EPR SPECTROSCOPY, ABSORPTION SPECTROSCOPY, SUBUNIT, SUBCELLULAR
RP LOCATION, AND PTM.
RC STRAIN=K12;
RX PubMed=17130127; DOI=10.1074/jbc.m607353200;
RA Jepson B.J., Mohan S., Clarke T.A., Gates A.J., Cole J.A., Butler C.S.,
RA Butt J.N., Hemmings A.M., Richardson D.J.;
RT "Spectropotentiometric and structural analysis of the periplasmic nitrate
RT reductase from Escherichia coli.";
RL J. Biol. Chem. 282:6425-6437(2007).
CC -!- FUNCTION: Electron transfer subunit of the periplasmic nitrate
CC reductase complex NapAB. Receives electrons from the membrane-anchored
CC tetraheme c-type NapC protein and transfers these to NapA subunit, thus
CC allowing electron flow between membrane and periplasm. Essential for
CC periplasmic nitrate reduction with nitrate as the terminal electron
CC acceptor. {ECO:0000269|PubMed:10234835, ECO:0000269|PubMed:10548535,
CC ECO:0000269|PubMed:17130127}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. The interaction between NapA and NapB is
CC weak. {ECO:0000269|PubMed:10234835, ECO:0000269|PubMed:17130127}.
CC -!- INTERACTION:
CC P0ABL3; P33937: napA; NbExp=2; IntAct=EBI-17171907, EBI-554952;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10234835,
CC ECO:0000269|PubMed:10548535, ECO:0000269|PubMed:17130127}.
CC -!- PTM: Binds 2 heme C groups per subunit.
CC -!- DISRUPTION PHENOTYPE: Deletion leads to reduced levels of formate- or
CC glycerol-dependent activity after anaerobic growth in the presence of
CC nitrate. {ECO:0000269|PubMed:10548535}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16395.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00008; AAA16395.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75263.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76666.1; -; Genomic_DNA.
DR RefSeq; NP_416707.4; NC_000913.3.
DR RefSeq; WP_000835174.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P0ABL3; -.
DR SMR; P0ABL3; -.
DR BioGRID; 4262224; 27.
DR ComplexPortal; CPX-3447; NapAB nitrate reductase complex.
DR IntAct; P0ABL3; 1.
DR STRING; 511145.b2203; -.
DR TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR jPOST; P0ABL3; -.
DR PaxDb; P0ABL3; -.
DR PRIDE; P0ABL3; -.
DR EnsemblBacteria; AAC75263; AAC75263; b2203.
DR EnsemblBacteria; BAE76666; BAE76666; BAE76666.
DR GeneID; 60669099; -.
DR GeneID; 946698; -.
DR KEGG; ecj:JW5367; -.
DR KEGG; eco:b2203; -.
DR PATRIC; fig|1411691.4.peg.33; -.
DR EchoBASE; EB1991; -.
DR eggNOG; COG3043; Bacteria.
DR HOGENOM; CLU_103367_3_0_6; -.
DR InParanoid; P0ABL3; -.
DR OMA; PIVPNEF; -.
DR PhylomeDB; P0ABL3; -.
DR BioCyc; EcoCyc:NAPB-MON; -.
DR BioCyc; MetaCyc:NAPB-MON; -.
DR BRENDA; 1.9.6.1; 2165.
DR PRO; PR:P0ABL3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009325; C:nitrate reductase complex; IPI:ComplexPortal.
DR GO; GO:0042597; C:periplasmic space; IDA:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0042128; P:nitrate assimilation; IC:ComplexPortal.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005591; NapB.
DR PANTHER; PTHR38604; PTHR38604; 1.
DR Pfam; PF03892; NapB; 1.
DR PIRSF; PIRSF006105; NapB; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:10234835"
FT CHAIN 28..149
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000006588"
FT BINDING 69
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 127..149
FT /note="HVPQADTAPIVGNTFTPSKGYGK -> QYRRPIPRQSWGIPLPHQKVTGNKR
FT LLWEILTVSLV (in Ref. 1; AAA16395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 149 AA; 16297 MW; 6F38F13C092178AF CRC64;
MKSHDLKKAL CQWTAMLALV VSGAVWAANG VDFSQSPEVS GTQEGAIRMP KEQDRMPLNY
VNQPPMIPHS VEGYQVTTNT NRCLQCHGVE SYRTTGAPRI SPTHFMDSDG KVGAEVAPRR
YFCLQCHVPQ ADTAPIVGNT FTPSKGYGK
