RCNA_SHIF8
ID RCNA_SHIF8 Reviewed; 282 AA.
AC Q0T333;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Nickel/cobalt efflux system RcnA;
GN Name=rcnA; OrderedLocusNames=SFV_2161;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(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; CP000266; ABF04282.1; -; Genomic_DNA.
DR RefSeq; WP_000134598.1; NC_008258.1.
DR AlphaFoldDB; Q0T333; -.
DR EnsemblBacteria; ABF04282; ABF04282; SFV_2161.
DR GeneID; 58389591; -.
DR KEGG; sfv:SFV_2161; -.
DR HOGENOM; CLU_058605_2_0_6; -.
DR OMA; HALEPGH; -.
DR BioCyc; SFLE373384:SFV_RS12110-MON; -.
DR Proteomes; UP000000659; 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..282
FT /note="Nickel/cobalt efflux system RcnA"
FT /id="PRO_0000333790"
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..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..217
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..282
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 127..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 282 AA; 31484 MW; 10AD0241E63D2EA8 CRC64;
MTEFTTLLQQ GNAWFFIPSA ILLGALHGLE PGHSKTMMAA FIIAIKGTIK QAVMLGLAAT
ISHTAVVWLI AFGGMVISKR FTAQSAEPWL QLISAVIIIG TAFWMFWRTW RGERNWLENM
HGHDYEHHHH HHDHEHHQDH EHHHDQGHHH HHEHGEYQDA HARAHANDIK RRFDGREVIN
WQILLFGLTG GFIPCPAAIT VLLICIQLKA LTLGATLVVS FSIGLALTLV TVGVGAAISV
QQVAKRWSGF NTLAKRAPYF SSLLIGLVGV YMGVHGFMGI MR
