NAPB_BRAJP
ID NAPB_BRAJP Reviewed; 167 AA.
AC Q8KY07;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB {ECO:0000250|UniProtKB:P39186};
DE Flags: Precursor;
GN Name=napB {ECO:0000312|EMBL:AAM47035.1};
OS Bradyrhizobium japonicum.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=375;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAM47035.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP INDUCTION, AND PTM.
RC STRAIN=USDA 110spc4 {ECO:0000312|EMBL:AAM47035.1};
RX PubMed=14663073; DOI=10.1099/mic.0.26620-0;
RA Delgado M., Bonnard N., Tresierra-Ayala A., Bedmar E.J., Muller P.;
RT "The Bradyrhizobium japonicum napEDABC genes encoding the periplasmic
RT nitrate reductase are essential for nitrate respiration.";
RL Microbiology 149:3395-3403(2003).
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:14663073}.
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:0000269|PubMed:14663073}.
CC -!- INDUCTION: Induced by anaerobic conditions, and further induced by
CC presence of nitrate. {ECO:0000269|PubMed:14663073}.
CC -!- PTM: Binds 2 heme C groups per subunit. {ECO:0000269|PubMed:14663073}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM47035.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF314590; AAM47035.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8KY07; -.
DR SMR; Q8KY07; -.
DR STRING; 1304878.AUGD01000001_gene40; -.
DR eggNOG; COG3043; Bacteria.
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 2: Evidence at transcript level;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW Transport.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..167
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000417029"
FT REGION 40..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79
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 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 96
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 97
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 114
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 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 136
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 137
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 167 AA; 18259 MW; CA06142157794935 CRC64;
MRRAHRAGER VMMKRFGIAL LAVAIAAGAS SLTAQTVTSG LHGPAPLNDE GPAPPMLPNR
NTSEREVRNY PEQPPVIPHT IDGYQVDLNG NKCLSCHARA RTAESQAPMV SITHFMDRDG
QFWPSISPRR FFCTECHVPQ NTATPPVSND FTDIDTLLSR ASPGGRR
