MCTB_MYCTU
ID MCTB_MYCTU Reviewed; 314 AA.
AC P9WJ83; L0TAD1; P58212; P64883;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 34.
DE RecName: Full=Copper transporter MctB;
DE AltName: Full=Mycobacterial copper transport protein B;
DE Flags: Precursor;
GN Name=mctB; OrderedLocusNames=Rv1698; ORFNames=MTCI125.20;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18434314; DOI=10.1074/jbc.m800866200;
RA Siroy A., Mailaender C., Harder D., Koerber S., Wolschendorf F.,
RA Danilchanka O., Wang Y., Heinz C., Niederweis M.;
RT "Rv1698 of Mycobacterium tuberculosis represents a new class of channel-
RT forming outer membrane proteins.";
RL J. Biol. Chem. 283:17827-17837(2008).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18439872; DOI=10.1016/j.tube.2008.02.004;
RA Song H., Sandie R., Wang Y., Andrade-Navarro M.A., Niederweis M.;
RT "Identification of outer membrane proteins of Mycobacterium tuberculosis.";
RL Tuberculosis 88:526-544(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21205886; DOI=10.1073/pnas.1009261108;
RA Wolschendorf F., Ackart D., Shrestha T.B., Hascall-Dove L., Nolan S.,
RA Lamichhane G., Wang Y., Bossmann S.H., Basaraba R.J., Niederweis M.;
RT "Copper resistance is essential for virulence of Mycobacterium
RT tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1621-1626(2011).
RN [6]
RP CRYSTALLIZATION.
RX PubMed=21045312; DOI=10.1107/s1744309110037644;
RA Chen L., Sun D., Wu M., Zang J., Tian C.;
RT "Cloning, expression, purification, crystallization and preliminary
RT crystallographic analysis of Rv1698, an outer membrane channel protein from
RT Mycobacterium tuberculosis.";
RL Acta Crystallogr. F 66:1525-1527(2010).
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. Required for
CC virulence. {ECO:0000269|PubMed:18434314, ECO:0000269|PubMed:21205886}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:18434314,
CC ECO:0000269|PubMed:18439872}.
CC -!- DISRUPTION PHENOTYPE: Mutants show a severe growth defect in the
CC presence of copper. Deletion causes a drastic virulence defect in
CC guinea pigs, mostly due to a much lower bacterial burden in the lungs.
CC {ECO:0000269|PubMed:21205886}.
CC -!- SIMILARITY: Belongs to the MctB (TC 1.B.50) family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44463.1; -; Genomic_DNA.
DR PIR; A70503; A70503.
DR RefSeq; NP_216214.1; NC_000962.3.
DR RefSeq; WP_003408390.1; NZ_NVQJ01000010.1.
DR AlphaFoldDB; P9WJ83; -.
DR STRING; 83332.Rv1698; -.
DR PaxDb; P9WJ83; -.
DR DNASU; 885047; -.
DR GeneID; 885047; -.
DR KEGG; mtu:Rv1698; -.
DR TubercuList; Rv1698; -.
DR eggNOG; ENOG5032TBA; Bacteria.
DR OMA; FRYHIVS; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:MTBBASE.
DR GO; GO:0046930; C:pore complex; IMP:MTBBASE.
DR GO; GO:0015288; F:porin activity; IDA:MTBBASE.
DR GO; GO:0055070; P:copper ion homeostasis; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IDA:MTBBASE.
DR InterPro; IPR021522; MctB.
DR Pfam; PF11382; MctB; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Copper; Ion transport; Membrane; Porin;
KW Reference proteome; Signal; Transmembrane; Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..314
FT /note="Copper transporter MctB"
FT /id="PRO_0000014105"
SQ SEQUENCE 314 AA; 32391 MW; 9B45A61E10F78339 CRC64;
MISLRQHAVS LAAVFLALAM GVVLGSGFFS DTLLSSLRSE KRDLYTQIDR LTDQRDALRE
KLSAADNFDI QVGSRIVHDA LVGKSVVIFR TPDAHDDDIA AVSKIVGQAG GAVTATVSLT
QEFVEANSAE KLRSVVNSSI LPAGSQLSTK LVDQGSQAGD LLGIALLSNA DPAAPTVEQA
QRDTVLAALR ETGFITYQPR DRIGTANATV VVTGGALSTD AGNQGVSVAR FAAALAPRGS
GTLLAGRDGS ANRPAAVAVT RADADMAAEI STVDDIDAEP GRITVILALH DLINGGHVGH
YGTGHGAMSV TVSQ
