Y1273_MYCTU
ID Y1273_MYCTU Reviewed; 582 AA.
AC P9WQJ1; L0T8W5; P0A4W4; Q11046;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein Rv1273c;
GN OrderedLocusNames=Rv1273c; ORFNames=MTCY50.09;
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 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44029.1; -; Genomic_DNA.
DR PIR; A70755; A70755.
DR RefSeq; NP_215789.1; NC_000962.3.
DR RefSeq; WP_003406574.1; NZ_NVQJ01000030.1.
DR AlphaFoldDB; P9WQJ1; -.
DR SMR; P9WQJ1; -.
DR STRING; 83332.Rv1273c; -.
DR PaxDb; P9WQJ1; -.
DR DNASU; 887025; -.
DR GeneID; 887025; -.
DR KEGG; mtu:Rv1273c; -.
DR TubercuList; Rv1273c; -.
DR eggNOG; COG1132; Bacteria.
DR OMA; MSVMMAT; -.
DR PhylomeDB; P9WQJ1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Uncharacterized ABC transporter ATP-binding protein
FT Rv1273c"
FT /id="PRO_0000093264"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 17..300
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 335..571
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 369..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 582 AA; 62116 MW; B9002E187776691F CRC64;
MLLALLRQHI RPYRRLVAML MMLQLVSTLA SLYLPTVNAA IVDDGVAKGD TATIVRLGAV
MLGVTGLQVL CAIGAVYLGS RTGAGFGRDL RSAMFEHIIT FSERETARFG APTLLTRSTN
DVRQILFLVQ MTATVLVTAP IMCVGGIIMA IHQEAALTWL LLVSVPILAV ANYWIISHML
PLFRRMQSLI DGINRVMRDQ LSGVRVVRAF TREGYERDKF AQANTALSNA ALSAGNWQAL
MLPVTTLTIN ASSVALIWFG GLRIDSGQMQ VGSLIAFLSY FAQILMAVLM ATMTLAVLPR
ASVCAERITE VLSTPAALGN PDNPKFPTDG VTGVVRLAGA TFTYPGADCP VLQDISLTAR
PGTTTAIVGS TGSGKSTLVS LICRLYDVTA GAVLVDGIDV REYHTERLWS AIGLVPQRSY
LFSGTVADNL RYGGGPDQVV TEQEMWEALR VAAADGFVQT DGLQTRVAQG GVNFSGGQRQ
RLAIARAVIR RPAIYVFDDA FSALDVHTDA KVHASLRQVS GDATIIVVTQ RISNAAQADQ
VIVVDNGKIV GTGTHETLLA DCPTYAEFAA SQSLSATVGG VG
