ID NIKO_RHOCB Reviewed; 254 AA. AC D5AQY6; DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot. DT 15-JUN-2010, sequence version 1. DT 21-MAR-2012, entry version 13. DE RecName: Full=Nickel import ATP-binding protein NikO; DE EC=3.6.3.-; DE AltName: Full=Energy-coupling factor transporter ATP-binding protein NikO; DE Short=ECF transporter A component NikO; GN Name=nikO; Synonyms=cbiO2; OrderedLocusNames=RCAP_rcc01032; OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=272942; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=20418398; DOI=10.1128/JB.00366-10; RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V., RA Haselkorn R.; RT "Complete genome sequence of the photosynthetic purple nonsulfur RT bacterium Rhodobacter capsulatus SB 1003."; RL J. Bacteriol. 192:3545-3546(2010). RN [2] RP FUNCTION IN NICKEL TRANSPORT, SUBSTRATES, SUBUNIT, AND EXPRESSION IN RP E.COLI. RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003; RX PubMed=16352848; DOI=10.1128/JB.188.1.317-327.2006; RA Rodionov D.A., Hebbeln P., Gelfand M.S., Eitinger T.; RT "Comparative and functional genomic analysis of prokaryotic nickel and RT cobalt uptake transporters: evidence for a novel group of ATP-binding RT cassette transporters."; RL J. Bacteriol. 188:317-327(2006). CC -!- FUNCTION: Part of the energy-coupling factor (ECF) transporter CC complex NikMNQO involved in nickel import. The complex confers CC nickel uptake upon expression in E.coli; can also transport cobalt CC with a very low affinity. Presumably responsible for energy CC coupling to the transport system. CC -!- SUBUNIT: Forms an energy-coupling factor (ECF) transporter complex CC composed of an ATP-binding protein (A component, NikO), a CC transmembrane protein (T component, NikQ) and a fused possible CC substrate-capture protein (S component, NikMN) of unknown CC stoichimetry (By similarity). CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC -!- SIMILARITY: Contains 1 ABC transporter domain. 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; CP001312; ADE84792.1; -; Genomic_DNA. DR RefSeq; YP_003577199.1; NC_014034.1. DR GeneID; 9003861; -. DR GenomeReviews; CP001312_GR; RCAP_rcc01032. DR KEGG; rcp:RCAP_rcc01032; -. DR PATRIC; 35502156; VBIRhoCap134200_1049. DR KO; K02006; -. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015675; P:nickel cation transport; IDA:UniProtKB. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome; KW Hydrolase; Ion transport; Membrane; Nickel; Nickel transport; KW Nucleotide-binding; Transport. FT CHAIN 1 254 Nickel import ATP-binding protein NikO. FT /FTId=PRO_0000411086. FT DOMAIN 5 246 ABC transporter. FT NP_BIND 37 44 ATP (Potential). SQ SEQUENCE 254 AA; 27039 MW; E1516853AD967B97 CRC64; MTPAFELQGV QFAYKGVPAL NGLDLTLPLG RRTALLGANG SGKSTLLRLL DGLQFPAAGR ISAFGTPLTE AMFTDEAAAI AFRRRVGFVF QNPEVQLFCP SVFDELAFGP LQLHWPKERI RARVARAIAQ FGLGPLAGRP PHRLSGGEKK RVALASVLIL DPEVLLLDEP TAALDPQATD DIAALLETEF GARNPGRTLI FSSHDLDLVA RIADHVVVLE AGKVAAAGPA AEVLARTALL RRARLLPGFD GTAP //