NAPB_WOLSU
ID NAPB_WOLSU Reviewed; 186 AA.
AC Q7M963; Q8GBF8;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB {ECO:0000250|UniProtKB:P44654};
DE Flags: Precursor;
GN Name=napB {ECO:0000312|EMBL:CAE10260.1}; OrderedLocusNames=WS1174;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAD55550.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=12823811; DOI=10.1046/j.1365-2958.2003.03544.x;
RA Simon J., Saenger M., Schuster S.C., Gross R.;
RT "Electron transport to periplasmic nitrate reductase (NapA) of Wolinella
RT succinogenes is independent of a NapC protein.";
RL Mol. Microbiol. 49:69-79(2003).
RN [2] {ECO:0000312|EMBL:CAE10260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
RN [3] {ECO:0000305}
RP FUNCTION, PTM, AND DISRUPTION PHENOTYPE.
RX PubMed=17975082; DOI=10.1099/mic.0.2007/009928-0;
RA Kern M., Mager A.M., Simon J.;
RT "Role of individual nap gene cluster products in NapC-independent nitrate
RT respiration of Wolinella succinogenes.";
RL Microbiology 153:3739-3747(2007).
CC -!- FUNCTION: Electron transfer subunit of the periplasmic nitrate
CC reductase complex NapAB. Transfers electrons 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:12823811, ECO:0000269|PubMed:17975082}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000250|UniProtKB:P44654}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P44654}.
CC -!- PTM: Binds 2 heme C groups per subunit. {ECO:0000269|PubMed:17975082}.
CC -!- DISRUPTION PHENOTYPE: Mutants fail to grow by nitrate respiration and
CC also fail to reduce nitrate and contain increased amounts of NapA.
CC {ECO:0000269|PubMed:17975082}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE10260.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ512686; CAD55550.1; -; Genomic_DNA.
DR EMBL; BX571660; CAE10260.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041571806.1; NC_005090.1.
DR AlphaFoldDB; Q7M963; -.
DR STRING; 273121.WS1174; -.
DR EnsemblBacteria; CAE10260; CAE10260; WS1174.
DR KEGG; wsu:WS1174; -.
DR eggNOG; COG3043; Bacteria.
DR HOGENOM; CLU_2385369_0_0_7; -.
DR OrthoDB; 1650975at2; -.
DR Proteomes; UP000000422; 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; IEA:InterPro.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005591; NapB.
DR PANTHER; PTHR38604; PTHR38604; 1.
DR Pfam; PF03892; NapB; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..186
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000417027"
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|UniProtKB:P44654"
FT BINDING 102
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 105
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 106
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 123
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 144
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 147
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 148
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 186 AA; 20626 MW; 7A2AC7B68D94C123 CRC64;
MKTSKLNFLT LVASTGLALA FLSGCTSNTG TTQSAKLYSE EELGLRKATI YNENKTLVKE
FEYSKEPAGA SKVYERSFEN APPMIPHDVE GMMDMSREIN MCTSCHLPEV AEAAAATPMP
KSHFFNMRTG EDLKGAMDEA RYNCSQCHTP QANVTPLVDN RFRPEFRGED AKNRSNLIDT
LNEGVK
