ID   NAPB_NEOGA              Reviewed;         163 AA.
AC   Q9Z3W3;
DT   16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE   AltName: Full=Diheme cytochrome c NapB {ECO:0000250|UniProtKB:Q53177, ECO:0000312|EMBL:AAD46690.1};
DE   Flags: Precursor;
GN   Name=napB {ECO:0000312|EMBL:AAC79444.1};
OS   Neorhizobium galegae (Rhizobium galegae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Neorhizobium.
OX   NCBI_TaxID=399;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC79444.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=G-179 {ECO:0000312|EMBL:AAC79444.1};
RX   PubMed=10217771; DOI=10.1128/jb.181.9.2802-2806.1999;
RA   Bedzyk L., Wang T., Ye R.W.;
RT   "The periplasmic nitrate reductase in Pseudomonas sp. strain G-179
RT   catalyzes the first step of denitrification.";
RL   J. Bacteriol. 181:2802-2806(1999).
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:10217771}.
CC   -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC       composed of NapA and NapB. {ECO:0000250|UniProtKB:Q53177}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10217771}.
CC   -!- PTM: Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:Q53177}.
CC   -!- SIMILARITY: Belongs to the NapB family. {ECO:0000255}.
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DR   EMBL; AF040988; AAD46690.1; -; Genomic_DNA.
DR   EMBL; AF083948; AAC79444.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Z3W3; -.
DR   SMR; Q9Z3W3; -.
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   PIRSF; PIRSF006105; NapB; 1.
DR   SUPFAM; SSF48695; SSF48695; 1.
DR   PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW   Transport.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..163
FT                   /note="Periplasmic nitrate reductase, electron transfer
FT                   subunit"
FT                   /id="PRO_0000417030"
FT   BINDING         76
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         90
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         93
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         94
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         111
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         130
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         133
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         134
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   163 AA;  18244 MW;  4082C2C5F5D31287 CRC64;
     MRSQDPSRRL SRRLWTLFAL ALCLVTGTVA LAQTVPQLSG RPSPMQNTGA DPLPRWIVDD
     IQKMRNYPDQ PPVIPHSIEG YQLSVNTNRC MSCHRRELTE GSGAPMISVT HYMNREGQML
     ADVSPRRYFC TACHVPQADT RPLVDNTFKD MSELGFKPAG SGQ