NAPB_CERSP
ID NAPB_CERSP Reviewed; 154 AA.
AC O88160;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB {ECO:0000250|UniProtKB:Q53177};
DE Flags: Precursor;
GN Name=napB {ECO:0000312|EMBL:AAC23523.1};
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAA31962.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=f. sp. denitrificans IL106 {ECO:0000312|EMBL:BAA31962.1};
RX PubMed=10227138; DOI=10.1271/bbb.63.530;
RA Liu H.P., Takio S., Satoh T., Yamamoto I.;
RT "Involvement in denitrification of the napKEFDABC genes encoding the
RT periplasmic nitrate reductase system in the denitrifying phototrophic
RT bacterium Rhodobacter sphaeroides f. sp. denitrificans.";
RL Biosci. Biotechnol. Biochem. 63:530-536(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC23523.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=f. sp. denitrificans IL106 {ECO:0000312|EMBL:AAC23523.1};
RX PubMed=10498715; DOI=10.1128/jb.181.19.6028-6032.1999;
RA Sabaty M., Schwintner C., Cahors S., Richaud P., Vermeglio A.;
RT "Nitrite and nitrous oxide reductase regulation by nitrogen oxides in
RT Rhodobacter sphaeroides f. sp. denitrificans IL106.";
RL J. Bacteriol. 181:6028-6032(1999).
RN [3] {ECO:0000305}
RP CRYSTALLIZATION, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=f. sp. denitrificans IL106 {ECO:0000269|PubMed:11717511};
RX PubMed=11717511; DOI=10.1107/s0907444901015852;
RA Pignol D., Adriano J.M., Fontecilla-Camps J.C., Sabaty M.;
RT "Crystallization and preliminary X-ray analysis of the periplasmic nitrate
RT reductase (NapA-NapB complex) from Rhodobacter sphaeroides f. sp.
RT denitrificans.";
RL Acta Crystallogr. D 57:1900-1902(2001).
RN [4] {ECO:0000305}
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=f. sp. denitrificans IL106 {ECO:0000269|PubMed:16136296};
RX PubMed=16136296; DOI=10.1007/s00203-005-0029-9;
RA Tabata A., Yamamoto I., Matsuzaki M., Satoh T.;
RT "Differential regulation of periplasmic nitrate reductase gene (napKEFDABC)
RT expression between aerobiosis and anaerobiosis with nitrate in a
RT denitrifying phototroph Rhodobacter sphaeroides f. sp. denitrificans.";
RL Arch. Microbiol. 184:108-116(2005).
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:10227138, ECO:0000269|PubMed:10498715,
CC ECO:0000269|PubMed:11717511, ECO:0000269|PubMed:16136296}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000269|PubMed:11717511}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:11717511}.
CC -!- INDUCTION: Induced at high levels by nitrate under anoxic conditions in
CC the dark. Induced by oxic conditions, even in the absence of nitrate.
CC It is suggested that the extent of electron flux to nitrate or oxygen,
CC under anoxic or oxic conditions, respectively, serves as the signal for
CC induction. {ECO:0000269|PubMed:16136296}.
CC -!- PTM: Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:Q53177}.
CC -!- DISRUPTION PHENOTYPE: Decrease in nitrate reductase activity in
CC deletion mutants and failure to grow in dark under anaerobic
CC conditions. {ECO:0000269|PubMed:10227138, ECO:0000269|PubMed:16136296}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000255}.
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DR EMBL; AB016290; BAA31962.1; -; Genomic_DNA.
DR EMBL; AF069545; AAC23523.1; -; Genomic_DNA.
DR AlphaFoldDB; O88160; -.
DR SMR; O88160; -.
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 1: Evidence at protein level;
KW Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..154
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_5000054350"
FT REGION 27..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 68
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 82
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 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 86
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 103
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 122
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 /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P44654"
FT BINDING 126
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 154 AA; 16948 MW; BDE8F1717E997075 CRC64;
MSMHPALRLL ATVLVALGAG PAFTQDAPRL TGADRPMSEV AAPPLPETIT DDRRVGRNYP
EQPPVIPHAI EGYQLSVNAN RCLECHRRQY SGLVAAPMIS ITHFQDREGQ MLADVSPRRY
FCTACHVPQT NAQPLVTNEF RDMLTLTPAS NEAE
