NAPB_PARPN
ID NAPB_PARPN Reviewed; 161 AA.
AC Q56351;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Cytochrome c552;
DE AltName: Full=Diheme cytochrome c NapB;
DE Flags: Precursor;
GN Name=napB;
OS Paracoccus pantotrophus (Thiosphaera pantotropha).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=82367;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 94-118 AND 131-152,
RP SUBUNIT, AND PTM.
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 / NCCB
RC 82005 / GB17;
RX PubMed=7639719; DOI=10.1042/bj3090983;
RA Berks B.C., Richardson D.J., Reilly A., Willis A.C., Ferguson S.J.;
RT "The napEDABC gene cluster encoding the periplasmic nitrate reductase
RT system of Thiosphaera pantotropha.";
RL Biochem. J. 309:983-992(1995).
RN [2]
RP FUNCTION, ABSORPTION SPECTROSCOPY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, PTM, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=M-6;
RX PubMed=8119278; DOI=10.1111/j.1432-1033.1994.tb18605.x;
RA Berks B.C., Richardson D.J., Robinson C., Reilly A., Aplin R.T.,
RA Ferguson S.J.;
RT "Purification and characterization of the periplasmic nitrate reductase
RT from Thiosphaera pantotropha.";
RL Eur. J. Biochem. 220:117-124(1994).
RN [3]
RP FUNCTION, EPR SPECTROSCOPY, AND PTM.
RC STRAIN=M-6;
RX PubMed=8194605; DOI=10.1016/0014-5793(94)00445-5;
RA Breton J., Berks B.C., Reilly A., Thomson A.J., Ferguson S.J.,
RA Richardson D.J.;
RT "Characterization of the paramagnetic iron-containing redox centres of
RT Thiosphaera pantotropha periplasmic nitrate reductase.";
RL FEBS Lett. 345:76-80(1994).
RN [4]
RP EPR SPECTROSCOPY, CIRCULAR DICHROISM, SUBUNIT, AND PTM.
RC STRAIN=M-6;
RX PubMed=11434929; DOI=10.1016/s0014-5793(01)02577-7;
RA Butler C.S., Ferguson S.J., Berks B.C., Thomson A.J., Cheesman M.R.,
RA Richardson D.J.;
RT "Assignment of haem ligands and detection of electronic absorption bands of
RT molybdenum in the di-haem periplasmic nitrate reductase of Paracoccus
RT pantotrophus.";
RL FEBS Lett. 500:71-74(2001).
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:8119278, ECO:0000269|PubMed:8194605}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are -15 mV and +80 mV. {ECO:0000269|PubMed:8119278};
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000269|PubMed:11434929,
CC ECO:0000269|PubMed:7639719, ECO:0000269|PubMed:8119278}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:8119278}.
CC -!- PTM: Binds 2 heme C groups per subunit.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000305}.
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DR EMBL; Z36773; CAA85347.1; -; Genomic_DNA.
DR PIR; S56136; S56136.
DR AlphaFoldDB; Q56351; -.
DR SMR; Q56351; -.
DR STRING; 935565.JAEM01000057_gene19; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW Periplasm; Pyrrolidone carboxylic acid; Signal; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..161
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000006590"
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:0000305"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250"
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:0000305"
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:0000305"
FT BINDING 133
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250"
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:0000305"
FT MOD_RES 30
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255"
SQ SEQUENCE 161 AA; 17789 MW; 29A4600F171E031F CRC64;
MRGQDPSRLI RPAAMAGLLL FALVGAALPQ AEPAVQIVPA LDRLGRADVR GQIPPLGRPI
TDDVRRMRNY PEQPPVIPHS IDGYQLTVNT NRCMDCHKPQ FTEGSGAPMI SVTHFQDRDG
QVLTDVTPRR YFCTACHVQQ TDVQPLVPNQ FRDGYRHAGG P
