NIKMN_RHOCB
ID NIKMN_RHOCB Reviewed; 347 AA.
AC D5AQY8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Fused nickel transport protein NikMN;
DE AltName: Full=Energy-coupling factor transporter probable substrate-capture protein NikMN;
DE Short=ECF transporter S component NikMN;
GN Name=nikMN; OrderedLocusNames=RCAP_rcc01034;
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 bacterium
RT 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 complex
CC NikMNQO involved in nickel import. The complex confers nickel uptake
CC upon expression in E.coli; can also transport cobalt with a very low
CC affinity. {ECO:0000269|PubMed:16352848}.
CC -!- SUBUNIT: Forms an energy-coupling factor (ECF) transporter complex
CC composed of an ATP-binding protein (A component, NikO), a transmembrane
CC protein (T component, NikQ) and a fused possible substrate-capture
CC protein (S component, NikMN) of unknown stoichimetry. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbiM family. NikM subfamily. {ECO:0000305}.
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DR EMBL; CP001312; ADE84794.1; -; Genomic_DNA.
DR RefSeq; WP_013066773.1; NC_014034.1.
DR AlphaFoldDB; D5AQY8; -.
DR SMR; D5AQY8; -.
DR STRING; 272942.RCAP_rcc01034; -.
DR TCDB; 3.A.1.23.7; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE84794; ADE84794; RCAP_rcc01034.
DR GeneID; 31489961; -.
DR KEGG; rcp:RCAP_rcc01034; -.
DR eggNOG; COG0310; Bacteria.
DR HOGENOM; CLU_052508_2_0_5; -.
DR OrthoDB; 1632785at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
DR GO; GO:0015675; P:nickel cation transport; IDA:UniProtKB.
DR InterPro; IPR002751; CbiM/NikMN.
DR InterPro; IPR025937; PDGLE_dom.
DR Pfam; PF01891; CbiM; 1.
DR Pfam; PF13190; PDGLE; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion transport; Membrane; Nickel;
KW Nickel transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..347
FT /note="Fused nickel transport protein NikMN"
FT /id="PRO_0000411083"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 347 AA; 35244 MW; 0A49A6DEB20BBBD3 CRC64;
MHIPDGYLSP VTCAVTFAAT VPFWYVSMRK LDRDLNGQHL PLVALVAAFS FVIMMFNLPI
PGGTTAHAAG IGIAAVLLGP WAAVPAISVA LLIQAIFFGD GGITAFGANC LNMAVVGPMV
AAAVYALGTR GAAIGSRRRV IMAGLASYAG LNAAALLAAV EFGVQPLFFH DAAGAPLYAP
YPLSVAVPAM ALTHLTIAGA AEFIVTAGLV AWLQRSNPEL LAPRRAPAAP ERHLRLWAGI
GALVVLCPLG LIAAGTAWGE WGAEDFTSEA GRAAMAGASG GVAPPAGLPG GFARLAELWS
APLPDYAPAF VQNAPLGYVL SALLGVALIV AGIGLSAGLR ALTRRAG