NAPB_CUPNH
ID NAPB_CUPNH Reviewed; 169 AA.
AC P39186;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Periplasmic nitrate reductase, electron transfer subunit;
DE AltName: Full=Diheme cytochrome c NapB;
DE Flags: Precursor;
GN Name=napB; OrderedLocusNames=PHG212;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-50, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RC PLASMID=megaplasmid pHG1;
RX PubMed=8376334; DOI=10.1128/jb.175.18.5867-5876.1993;
RA Siddiqui R.A., Warnecke-Eberz U., Hengsberger A., Schneider B., Kostka S.,
RA Friedrich B.;
RT "Structure and function of a periplasmic nitrate reductase in Alcaligenes
RT eutrophus H16.";
RL J. Bacteriol. 175:5867-5876(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
RN [3]
RP CRYSTALLIZATION, SUBUNIT, SUBCELLULAR LOCATION, AND PTM.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RC PLASMID=megaplasmid pHG1;
RX PubMed=17554176; DOI=10.1107/s1744309107022129;
RA Coelho C., Gonzalez P.J., Trincao J., Carvalho A.L., Najmudin S.,
RA Hettman T., Dieckman S., Moura J.J., Moura I., Romao M.J.;
RT "Heterodimeric nitrate reductase (NapAB) from Cupriavidus necator H16:
RT purification, crystallization and preliminary X-ray analysis.";
RL Acta Crystallogr. F 63:516-519(2007).
RN [4] {ECO:0007744|PDB:3ML1, ECO:0007744|PDB:3O5A}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 35-169 IN COMPLEX WITH NAPA AND
RP HEME C, EPR SPECTROSCOPY, ABSORPTION SPECTROSCOPY, SUBUNIT, SUBCELLULAR
RP LOCATION, AND PTM.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RC PLASMID=megaplasmid pHG1;
RX PubMed=21419779; DOI=10.1016/j.jmb.2011.03.016;
RA Coelho C., Gonzalez P.J., Moura J.G., Moura I., Trincao J., Joao Romao M.;
RT "The crystal structure of Cupriavidus necator nitrate reductase in oxidized
RT and partially reduced states.";
RL J. Mol. Biol. 408:932-948(2011).
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:8376334}.
CC -!- SUBUNIT: Component of the periplasmic nitrate reductase NapAB complex
CC composed of NapA and NapB. {ECO:0000269|PubMed:17554176,
CC ECO:0000269|PubMed:21419779, ECO:0000269|PubMed:8376334}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:17554176,
CC ECO:0000269|PubMed:21419779}.
CC -!- INDUCTION: Expressed independently of nitrate induction and
CC anaerobiosis.
CC -!- PTM: Binds 2 heme C groups per subunit.
CC -!- SIMILARITY: Belongs to the NapB family. {ECO:0000305}.
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DR EMBL; X71385; CAA50508.1; -; Genomic_DNA.
DR EMBL; AY305378; AAP85964.1; -; Genomic_DNA.
DR PIR; B48489; B48489.
DR RefSeq; WP_011154127.1; NZ_CP039289.1.
DR PDB; 3ML1; X-ray; 1.60 A; B=35-169.
DR PDB; 3O5A; X-ray; 1.72 A; B=35-169.
DR PDBsum; 3ML1; -.
DR PDBsum; 3O5A; -.
DR AlphaFoldDB; P39186; -.
DR SMR; P39186; -.
DR STRING; 381666.PHG212; -.
DR EnsemblBacteria; AAP85964; AAP85964; PHG212.
DR GeneID; 39976367; -.
DR KEGG; reh:PHG212; -.
DR PATRIC; fig|381666.6.peg.160; -.
DR eggNOG; COG3043; Bacteria.
DR HOGENOM; CLU_103367_2_0_4; -.
DR OMA; KCMSCHA; -.
DR OrthoDB; 1650975at2; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Plasmid; Reference proteome; Signal; Transport.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:8376334"
FT CHAIN 36..169
FT /note="Periplasmic nitrate reductase, electron transfer
FT subunit"
FT /id="PRO_0000006587"
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:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
FT BINDING 96
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
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:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
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:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
FT BINDING 133
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
FT BINDING 136
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
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:0000269|PubMed:21419779,
FT ECO:0007744|PDB:3ML1"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:3ML1"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3ML1"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:3ML1"
SQ SEQUENCE 169 AA; 18924 MW; 186AA597E012232D CRC64;
MKPSRSWASL LAVCAVLLAA LAMQAIFFPA PARAQGLVDA MRGPTAIANE PRAPLLYPTE
NKDIRRTRNY TMQPPTIPHK IDGYQLDKDF NRCMFCHART RTEETQAIPV SITHYMDRDN
NVLADVSPRR YFCTQCHVPQ ADTKPLIGNN FVDVDTILKR RPGAKGAAK
