NAPB_SHEON
ID NAPB_SHEON Reviewed; 143 AA.
AC Q8EIJ4;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB {ECO:0000303|PubMed:19387485, ECO:0000312|EMBL:AAN53921.1};
DE Flags: Precursor;
GN Name=napB {ECO:0000312|EMBL:AAN53921.1}; OrderedLocusNames=SO_0845;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1] {ECO:0000312|EMBL:AAN53921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2] {ECO:0000305}
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MR-1 {ECO:0000269|PubMed:19387485};
RX PubMed=19387485; DOI=10.1038/ismej.2009.40;
RA Gao H., Yang Z.K., Barua S., Reed S.B., Romine M.F., Nealson K.H.,
RA Fredrickson J.K., Tiedje J.M., Zhou J.;
RT "Reduction of nitrate in Shewanella oneidensis depends on atypical NAP and
RT NRF systems with NapB as a preferred electron transport protein from CymA
RT to NapA.";
RL ISME J. 3:966-976(2009).
CC -!- FUNCTION: Electron transfer subunit of the periplasmic nitrate
CC reductase complex NapAB. Receives electrons from the membrane-anchored
CC tetraheme c-type CymA protein and transfers these to NapA subunit, thus
CC allowing electron flow between membrane and periplasm. Not essential
CC for nitrate reduction but confers advantage to the organism when grown
CC on nitrate and thereby a fitness gain in utilizing nitrate.
CC {ECO:0000269|PubMed:19387485}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000250|UniProtKB:P39186}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P39186}.
CC -!- INDUCTION: By nitrate or fumarate under anaerobic conditions.
CC {ECO:0000269|PubMed:19387485}.
CC -!- PTM: Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:P39186}.
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit 15% slower rate of nitrate
CC reduction compared to mutants for other genes in the NAP operon.
CC Mutants can grow on nitrate to maximum cell density earlier than wild-
CC type. Nitrite is not detected in mutant strains but ammonium reaches
CC detectable levels sooner than in wild-type and accumulates to same
CC level as in wild-type. Double mutants with deletions of both NapA and
CC NapB fail to grow on nitrate or reduce nitrate under anaerobic
CC conditions. Double mutants for both NapB and NrfA reduces nitrate as
CC fast as wild-type. {ECO:0000269|PubMed:19387485}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000255}.
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DR EMBL; AE014299; AAN53921.1; -; Genomic_DNA.
DR RefSeq; NP_716476.1; NC_004347.2.
DR RefSeq; WP_011071135.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EIJ4; -.
DR STRING; 211586.SO_0845; -.
DR PaxDb; Q8EIJ4; -.
DR KEGG; son:SO_0845; -.
DR PATRIC; fig|211586.12.peg.809; -.
DR eggNOG; COG3043; Bacteria.
DR HOGENOM; CLU_103367_1_0_6; -.
DR OMA; CLTCHSW; -.
DR OrthoDB; 1650975at2; -.
DR PhylomeDB; Q8EIJ4; -.
DR BioCyc; SONE211586:G1GMP-787-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..143
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000417028"
FT BINDING 72
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|UniProtKB:P44654"
FT BINDING 85
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P44654"
FT BINDING 88
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P44654"
FT BINDING 89
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|UniProtKB:P44654"
FT BINDING 106
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|UniProtKB:P44654"
FT BINDING 121
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P44654"
FT BINDING 124
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P44654"
FT BINDING 125
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|UniProtKB:P44654"
SQ SEQUENCE 143 AA; 15432 MW; 282E7AFD32EA8380 CRC64;
MKKILTLAAI VLAIGGCSGQ QAETQATPVN IKSLAGDSAV TDIRPADAMP VYPARGKALE
RSFTDQPPLI PHKDDYKITL DKNGCLTCHS WDKAARMKAT PVAKSHVIDD KGTLNGHNYF
CTQCHVAQAE NKAPLVENKF STQ
