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 27-MAR-2024, entry version 141. 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; Pseudomonadota; 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 RC 337; 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 RC 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 RC 337; 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 RC 337; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 OrthoDB; 13290at2; -. 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; PERIPLASMIC NITRATE REDUCTASE, ELECTRON TRANSFER SUBUNIT; 1. DR PANTHER; PTHR38604:SF1; PERIPLASMIC NITRATE REDUCTASE, ELECTRON TRANSFER SUBUNIT; 1. DR Pfam; PF03892; NapB; 1. DR PIRSF; PIRSF006105; NapB; 1. DR SUPFAM; SSF48695; Multiheme cytochromes; 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 //