NAPB_CERS4
ID NAPB_CERS4 Reviewed; 154 AA.
AC Q53177; Q3IV42;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB;
DE Flags: Precursor;
GN Name=napB; OrderedLocusNames=RHOS4_40240; ORFNames=RSP_4117;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OG Plasmid pRS241c.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.; PLASMID=pRS241c;
RX PubMed=8730872; DOI=10.1111/j.1365-2958.1996.tb02475.x;
RA Reyes F., Roldan M.D., Klipp W., Castillo F., Moreno-Vivian C.;
RT "Isolation of periplasmic nitrate reductase genes from Rhodobacter
RT sphaeroides DSM 158: structural and functional differences among
RT prokaryotic nitrate reductases.";
RL Mol. Microbiol. 19:1307-1318(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.; PLASMID=pRS241c;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of plasmid C of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 25-154 IN COMPLEX WITH NAPA AND
RP HEME C, FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.; PLASMID=pRS241c;
RX PubMed=14528294; DOI=10.1038/nsb994;
RA Arnoux P., Sabaty M., Alric J., Frangioni B., Guigliarelli B.,
RA Adriano J.-M., Pignol D.;
RT "Structural and redox plasticity in the heterodimeric periplasmic nitrate
RT reductase.";
RL Nat. Struct. Biol. 10:928-934(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:14528294, ECO:0000269|PubMed:8730872}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000269|PubMed:14528294}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Induced by nitrate. Not repressed by ammonium or oxygen.
CC -!- PTM: Binds 2 heme C groups per subunit.
CC -!- DISRUPTION PHENOTYPE: Deletion mutants show reduced nitrate reductase
CC activity. {ECO:0000269|PubMed:8730872}.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000305}.
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DR EMBL; Z46806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP000146; ABA81592.1; -; Genomic_DNA.
DR RefSeq; WP_011331399.1; NZ_CP030275.1.
DR RefSeq; YP_345333.1; NC_007489.1.
DR PDB; 1OGY; X-ray; 3.20 A; B/D/F/H/J/L/N/P=25-154.
DR PDBsum; 1OGY; -.
DR AlphaFoldDB; Q53177; -.
DR SMR; Q53177; -.
DR IntAct; Q53177; 1.
DR EnsemblBacteria; ABA81592; ABA81592; RSP_4117.
DR KEGG; rsp:RSP_4117; -.
DR PATRIC; fig|272943.9.peg.179; -.
DR OMA; FCTACHV; -.
DR PhylomeDB; Q53177; -.
DR EvolutionaryTrace; Q53177; -.
DR Proteomes; UP000002703; Plasmid pRS241c.
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 3D-structure; Electron transport; Heme; Iron; Metal-binding; Periplasm;
KW Plasmid; Pyrrolidone carboxylic acid; Reference proteome; 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_0000006591"
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 BINDING 82
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:14528294"
FT BINDING 85
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:14528294"
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 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 BINDING 122
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:14528294"
FT BINDING 125
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:14528294"
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 MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000255"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1OGY"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1OGY"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1OGY"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1OGY"
SQ SEQUENCE 154 AA; 16908 MW; 63CE7404A5864977 CRC64;
MSVHPTLRFL ATALVALGAG AALAQDAPRL TGADRPMSEV AAPPLPETIT DDRRVGRNYP
EQPPVIPHSI EGYQLSVNAN RCLECHRRQY SGLVAAPMIS ITHFQDREGQ MLADVSPRRY
FCTACHVPQT NAQPLVTNEF RDMLTLMPAS NEAE
