RCNA_ECOUT
ID RCNA_ECOUT Reviewed; 274 AA.
AC Q1R9W6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Nickel/cobalt efflux system RcnA;
GN Name=rcnA; OrderedLocusNames=UTI89_C2380;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE07848.1; -; Genomic_DNA.
DR RefSeq; WP_000134614.1; NC_007946.1.
DR AlphaFoldDB; Q1R9W6; -.
DR EnsemblBacteria; ABE07848; ABE07848; UTI89_C2380.
DR KEGG; eci:UTI89_C2380; -.
DR HOGENOM; CLU_058605_2_0_6; -.
DR OMA; HALEPGH; -.
DR Proteomes; UP000001952; 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_0000333783"
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