Y987_MYCTU
ID Y987_MYCTU Reviewed; 855 AA.
AC O53900; F2GHT9; I6WZZ1; L0T8A8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Uncharacterized ABC transporter permease protein Rv0987 {ECO:0000305};
GN OrderedLocusNames=Rv0987 {ECO:0000312|EMBL:CCP43737.1};
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 FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16586367; DOI=10.1086/502631;
RA Jain S.K., Paul-Satyaseela M., Lamichhane G., Kim K.S., Bishai W.R.;
RT "Mycobacterium tuberculosis invasion and traversal across an in vitro human
RT blood-brain barrier as a pathogenic mechanism for central nervous system
RT tuberculosis.";
RL J. Infect. Dis. 193:1287-1295(2006).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=MT103;
RX PubMed=17030567; DOI=10.1128/iai.00058-06;
RA Rosas-Magallanes V., Stadthagen-Gomez G., Rauzier J., Barreiro L.B.,
RA Tailleux L., Boudou F., Griffin R., Nigou J., Jackson M., Gicquel B.,
RA Neyrolles O.;
RT "Signature-tagged transposon mutagenesis identifies novel Mycobacterium
RT tuberculosis genes involved in the parasitism of human macrophages.";
RL Infect. Immun. 75:504-507(2007).
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).
CC -!- FUNCTION: Probably part of an ABC transporter complex involved in host
CC cell binding either through secretion of an adherence factor or through
CC maintaining the architecture and integrity of the mycobacterial cell
CC envelope (PubMed:17030567). Could be required for host endothelial-cell
CC invasion and/or intracellular survival (PubMed:16586367).
CC {ECO:0000269|PubMed:16586367, ECO:0000269|PubMed:17030567}.
CC -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC (Rv0986) and two transmembrane proteins (Rv0987). {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Highly up-regulated during the early stages of invasion of
CC the human blood-brain barrier. {ECO:0000269|PubMed:16586367}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene reduces the ability of
CC M.tuberculosis to bind to host cells. Disruption does not reduce
CC virulence in a mouse model of infection (PubMed:17030567). Invasion of
CC the infant human brain microvascular endothelial-cell monolayer is
CC significantly decreased in transposon mutant (PubMed:16586367).
CC {ECO:0000269|PubMed:16586367, ECO:0000269|PubMed:17030567}.
CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43737.1; -; Genomic_DNA.
DR RefSeq; NP_215502.1; NC_000962.3.
DR RefSeq; WP_003915882.1; NZ_NVQJ01000018.1.
DR AlphaFoldDB; O53900; -.
DR SMR; O53900; -.
DR STRING; 83332.Rv0987; -.
DR PaxDb; O53900; -.
DR DNASU; 885363; -.
DR GeneID; 885363; -.
DR KEGG; mtu:Rv0987; -.
DR PATRIC; fig|83332.111.peg.1095; -.
DR TubercuList; Rv0987; -.
DR eggNOG; COG0577; Bacteria.
DR OMA; LIMWRLS; -.
DR PhylomeDB; O53900; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR InterPro; IPR003838; ABC3_permease_dom.
DR InterPro; IPR025857; MacB_PCD.
DR Pfam; PF02687; FtsX; 2.
DR Pfam; PF12704; MacB_PCD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..855
FT /note="Uncharacterized ABC transporter permease protein
FT Rv0987"
FT /id="PRO_0000451251"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 855 AA; 93606 MW; 4318B0E4E5F818B5 CRC64;
MNDQAPVAYA PLWRTAWRRL RQRPFQYILL VLGIALGVAM IVAIDVSSNS AQRAFDLSAA
AITGKSTHRL VSGPAGVDQQ LYVDLRRHGY DFSAPVIEGY VLARGLGNRA MQFMGTDPFA
ESAFRSPLWS NQNIAELGGF LTRPNGVVLS RQVAQKYGLA VGDRIALQVK GAPTTVTLVG
LLTPADEVSN QKLSDLIIAD ISTAQELFHM PGRLSHIDLI IKDEATATRI QQRLPAGVRM
ETSDTQRDTV KQMTDAFTVN LTALSLIALL VGIFLIYNTV TFNVVQRRPF FAILRCLGVT
REQLFWLIMT ESLVAGLIGT GLGLLIGIWL GEGLIGLVTQ TINDFYFVIN VRNVSVSAES
LLKGLIIGIF AAMLATLPPA IEAMRTVPAS TLRRSSLESK ITKLMPWLWV AWFGLGSFGV
LMLWLPGNNL VVAFVGLFSV LIALALIAPP LTRFVMLRLA PGLGRLLGPI GRMAPRNIVR
SLSRTSIAIA ALMMAVSLMV GVSISVGSFR QTLANWLEVT LKSDVYVSPP TLTSGRPSGN
LPVDAVRNIS KWPGVRDAVM ARYSSVFAPD WGREVELMAV SGDISDGKRP YRWIDGNKDT
LWPRFLAGKG VMLSEPMVSR QHLQMPPRPI TLMTDSGPQT FPVLAVFSDY TSDQGVILMD
RASYRAHWQD DDVTTMFLFL ASGANSGALI DQLQAAFAGR EDIVIQSTHS VREASMFIFD
RSFTITIALQ LVATVVAFIG VLSALMSLEL DRAHELGVFR AIGMTTRQLW KLMFIETGLM
GGMAGLMALP TGCILAWILV RIINVRSFGW TLQMHFESAH FLRALLVAVV AALAAGMYPA
WRLGRMTIRT AIREE
