RCNA_SHIDS
ID RCNA_SHIDS Reviewed; 285 AA.
AC Q32E98;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Nickel/cobalt efflux system RcnA;
GN Name=rcnA; OrderedLocusNames=SDY_2280;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62357.1; -; Genomic_DNA.
DR RefSeq; WP_000134651.1; NC_007606.1.
DR RefSeq; YP_403848.1; NC_007606.1.
DR AlphaFoldDB; Q32E98; -.
DR STRING; 300267.SDY_2280; -.
DR EnsemblBacteria; ABB62357; ABB62357; SDY_2280.
DR KEGG; sdy:SDY_2280; -.
DR PATRIC; fig|300267.13.peg.2753; -.
DR HOGENOM; CLU_058605_2_0_6; -.
DR OMA; HALEPGH; -.
DR Proteomes; UP000002716; 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; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..285
FT /note="Nickel/cobalt efflux system RcnA"
FT /id="PRO_0000333789"
FT TOPO_DOM 1..10
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..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..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..220
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 242..262
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..285
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 127..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 285 AA; 31864 MW; 04415A588F3AF5AF CRC64;
MTEFTTLLQQ GSAWFFIPSA ILLGALHGLE PGHSKTMMAA FIIAIKGTIK QAVMLGLAAT
ISHTAVVWLI AFGGMVISKR FTAQSAEPWL QLISAVIIIS TAFWMFWRTW RGERNWLENM
HEHEHDHEHH HHDHEHHQDH DHDHDHEHHH HHEHGDNEEY QDAHARAHAN DIKRHFDGRE
VTNWQILLFG LTGGLIPCPA AITVLLICIQ LKALTLGATL VVSFSIGLAL TLVTVGVGAA
ISVQQVAKRW SGFNTLAKRA PYFSSLLIGL VGVYMGVHGF MGIMR