RCNA_ECOK1
ID RCNA_ECOK1 Reviewed; 274 AA.
AC A1ACX1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Nickel/cobalt efflux system RcnA;
GN Name=rcnA; OrderedLocusNames=Ecok1_20170; ORFNames=APECO1_4440;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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}.
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DR EMBL; CP000468; ABJ01511.1; -; Genomic_DNA.
DR RefSeq; WP_000134614.1; NC_008563.1.
DR AlphaFoldDB; A1ACX1; -.
DR EnsemblBacteria; ABJ01511; ABJ01511; APECO1_4440.
DR KEGG; ecv:APECO1_4440; -.
DR HOGENOM; CLU_058605_2_0_6; -.
DR OMA; HALEPGH; -.
DR Proteomes; UP000008216; 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_0000333784"
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..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..86
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..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 127..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 274 AA; 30443 MW; E7DE83A21EA2792D CRC64;
MTEFTTLLQQ GNAWFFIPSA ILLGALHGLE PGHSKTMMAA FIIAIKGTIK QAVMLGLAAT
ISHTAVVWLI AFGGMVISKR FTAQSAEPWL QLISAVIIIS TAFWMFWRTW RGERNWLENM
HEHDHEHHHH DHEDHHDHGH HHHHEHGEYQ DAHARAHAND IKRRFDGREV TNWQILLFGL
TGGLIPCPAA ITVLLICIQL KALTLGATLV VSFSLGLALT LVTVGVGAAI SVQQVAKRWS
GFNTLAKRAP YFSSLLIGLV GVYMGVHGFM GIMR