MCTB_MYCLE
ID MCTB_MYCLE Reviewed; 317 AA.
AC Q49894; O05673; Q49893;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Copper transporter MctB;
DE Flags: Precursor;
GN Name=mctB; OrderedLocusNames=ML1362; ORFNames=MLC1351.10c, u0247f;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Pore-forming protein, which is involved in efflux of copper
CC across the outer membrane. Essential for copper resistance and
CC maintenance of a low intracellular copper concentration (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MctB (TC 1.B.50) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50924.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00021; AAA50908.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00021; AAA50924.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z95117; CAB08274.1; -; Genomic_DNA.
DR EMBL; AL583921; CAC31743.1; -; Genomic_DNA.
DR PIR; D87079; D87079.
DR PIR; S72963; S72963.
DR PIR; S72964; S72964.
DR RefSeq; NP_301972.1; NC_002677.1.
DR RefSeq; WP_010908293.1; NC_002677.1.
DR AlphaFoldDB; Q49894; -.
DR SMR; Q49894; -.
DR STRING; 272631.ML1362; -.
DR EnsemblBacteria; CAC31743; CAC31743; CAC31743.
DR KEGG; mle:ML1362; -.
DR PATRIC; fig|272631.5.peg.2519; -.
DR Leproma; ML1362; -.
DR eggNOG; ENOG5032TBA; Bacteria.
DR HOGENOM; CLU_072020_0_1_11; -.
DR OMA; FRYHIVS; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0055070; P:copper ion homeostasis; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR021522; MctB.
DR Pfam; PF11382; MctB; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Copper; Ion transport; Membrane; Porin;
KW Reference proteome; Signal; Transmembrane; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..317
FT /note="Copper transporter MctB"
FT /id="PRO_0000014107"
SQ SEQUENCE 317 AA; 32360 MW; 2C52D7BC503F9416 CRC64;
MISLRQHAFS LAAVFLALAV GVVLGSGFLS DTLLSSLRDE KRDLYTQISG LNDQKNMLNE
KVSAANNFDN QLLGRIVHDV LGGTSVVVFR TPDAKDDDVA AVSKIVVQAG GTVTGTVSLT
QEFVDANSTE KLRSVVNSSI LPAGAQLSTK LVDQGSQAGD LLGITLLVNA NPAVPNVGDA
QRSTVLVALR DTGFITYQTY NRNDHLGAAN AALVITGGLL PQDAGNQGVS VARFSAALAP
HGSGTLLAGR DGSATGVAAV AVARADAGMA ATISTVDNVD AEPGRITAIL GLHDLLSGGH
TGQYGVGHGA TSITVPQ