RCNA_SALPA
ID RCNA_SALPA Reviewed; 274 AA.
AC Q5PEQ4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Nickel/cobalt efflux system RcnA;
GN Name=rcnA; OrderedLocusNames=SPA2891;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
CC -!- FUNCTION: Efflux system for nickel and cobalt. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By nickel and cobalt. Transcriptionally repressed by RcnR
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family. RcnA
CC subfamily. {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; CP000026; AAV78734.1; -; Genomic_DNA.
DR RefSeq; WP_000503619.1; NC_006511.1.
DR AlphaFoldDB; Q5PEQ4; -.
DR EnsemblBacteria; AAV78734; AAV78734; SPA2891.
DR KEGG; spt:SPA2891; -.
DR HOGENOM; CLU_058605_2_0_6; -.
DR OMA; HALEPGH; -.
DR Proteomes; UP000008185; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR011541; Ni/Co_transpt_high_affinity.
DR Pfam; PF03824; NicO; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cobalt; Cobalt transport;
KW Ion transport; Membrane; Nickel; Nickel transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..274
FT /note="Nickel/cobalt efflux system RcnA"
FT /id="PRO_0000194012"
FT TOPO_DOM 1..12
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..85
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..209
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..274
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 122..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 29816 MW; DEF428B1A4B2501D CRC64;
MGEFPTLLQQ GNGWFFIPSA ILLGILHGLE PGHSKTMMAA FIIAIKGTVK QAVMLGLAAT
LSHTAIVWLI ALGGMYLSRA FTAQSVEPWL QLISAIIILS TACWMFWRTW RGEQQWLAGN
HHHDHDHDHD HDHDHHGHIH PEGATSKAYQ DAHERAHAAD IQRRFDGQTV TNGQILLFGL
TGGLIPCPAA ITVLLICIQL KAFTLGATMV LSFSLSLALT LVTVGVGAAI SVQQAAKRWS
GFSTLARRAP YFSSILIGLV GVYMGIHGYT GIMQ