BACA_MYCTU
ID BACA_MYCTU Reviewed; 639 AA.
AC P9WQI9; L0TAH3; Q50614;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Hydrophilic compounds import ATP-binding/permease protein BacA {ECO:0000305};
DE EC=7.6.2.- {ECO:0000305|PubMed:32296172};
DE AltName: Full=Hydrophilic compounds ABC transporter BacA {ECO:0000305};
GN Name=bacA {ECO:0000303|PubMed:18996991}; OrderedLocusNames=Rv1819c;
GN ORFNames=MTCY1A11.24c;
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 IN VIRULENCE, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=18996991; DOI=10.1128/jb.01132-08;
RA Domenech P., Kobayashi H., LeVier K., Walker G.C., Barry C.E. III;
RT "BacA, an ABC transporter involved in maintenance of chronic murine
RT infections with Mycobacterium tuberculosis.";
RL J. Bacteriol. 191:477-485(2009).
RN [3]
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 [4]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND MODELING.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23407640; DOI=10.1098/rsob.120175;
RA Gopinath K., Venclovas C., Ioerger T.R., Sacchettini J.C., McKinney J.D.,
RA Mizrahi V., Warner D.F.;
RT "A vitamin B12 transporter in Mycobacterium tuberculosis.";
RL Open Biol. 3:120175-120175(2013).
RN [5] {ECO:0007744|PDB:6TQE, ECO:0007744|PDB:6TQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.5 ANGSTROMS) OF MUTANT GLY-576 IN
RP COMPLEXES WITH ATP AND NON-HYDROLYSABLE ATP ANALOG, FUNCTION, ATPASE
RP ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF GLU-576.
RX PubMed=32296172; DOI=10.1038/s41586-020-2072-8;
RA Rempel S., Gati C., Nijland M., Thangaratnarajah C., Karyolaimos A.,
RA de Gier J.W., Guskov A., Slotboom D.J.;
RT "A mycobacterial ABC transporter mediates the uptake of hydrophilic
RT compounds.";
RL Nature 580:409-412(2020).
CC -!- FUNCTION: Multi-solute ABC transporter that mediates uptake of
CC unrelated hydrophilic compounds (PubMed:32296172). Can transport
CC vitamin B12 and related corrinoids, and antimicrobial peptides such as
CC bleomycin (PubMed:18996991, PubMed:32296172, PubMed:23407640).
CC Transmembrane domains (TMD) form a pore in the membrane and the ATP-
CC binding domain (NBD) is responsible for energy generation
CC (PubMed:32296172). Contributes to maintenance of chronic infections
CC (PubMed:18996991). {ECO:0000269|PubMed:18996991,
CC ECO:0000269|PubMed:23407640, ECO:0000269|PubMed:32296172}.
CC -!- ACTIVITY REGULATION: The presence of cobalamin does not affect the
CC ATPase activity. {ECO:0000269|PubMed:32296172}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:32296172,
CC ECO:0000305|PubMed:23407640}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32296172};
CC Multi-pass membrane protein {ECO:0000269|PubMed:32296172}.
CC -!- DOMAIN: Contains a large occluded hydrophilic cavity that spans the
CC entire thickness of the membrane and extends into the intracellular
CC part of the protein. It consists of two connected chambers. The larger
CC chamber is located in the transmembrane domain, and the smaller chamber
CC is formed by the part of the protein that connects the NBDs and
CC transmembrane domains. {ECO:0000269|PubMed:32296172}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in bleomycin resistance and
CC alters the outcome of a chronic infection within the host, but does not
CC alter sensitivity to other membrane-disrupting agents and resistance to
CC clinically important antituberculosis drugs (PubMed:18996991). Deletion
CC eliminates the ability of the bacterium to transport vitamin B12 and
CC related corrinoids (PubMed:23407640). {ECO:0000269|PubMed:18996991,
CC ECO:0000269|PubMed:23407640}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP44585.1; -; Genomic_DNA.
DR PIR; D70720; D70720.
DR RefSeq; NP_216335.1; NC_000962.3.
DR RefSeq; WP_003900416.1; NZ_NVQJ01000013.1.
DR PDB; 6TQE; EM; 4.30 A; A/B=1-639.
DR PDB; 6TQF; EM; 3.50 A; A/B=1-639.
DR PDBsum; 6TQE; -.
DR PDBsum; 6TQF; -.
DR AlphaFoldDB; P9WQI9; -.
DR SMR; P9WQI9; -.
DR STRING; 83332.Rv1819c; -.
DR PaxDb; P9WQI9; -.
DR GeneID; 885539; -.
DR KEGG; mtu:Rv1819c; -.
DR PATRIC; fig|83332.111.peg.2024; -.
DR TubercuList; Rv1819c; -.
DR eggNOG; COG4178; Bacteria.
DR OMA; FRYGLVH; -.
DR PhylomeDB; P9WQI9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0052572; P:response to host immune response; IMP:MTBBASE.
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 Pfam; PF06472; ABC_membrane_2; 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; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..639
FT /note="Hydrophilic compounds import ATP-binding/permease
FT protein BacA"
FT /id="PRO_0000093265"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 67..393
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 427..639
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 462..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32296172"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:32296172"
FT MUTAGEN 576
FT /note="E->G: Loss of cobalamin transport. Shows background
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:32296172"
FT TURN 16..20
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 21..34
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 38..42
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 46..50
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 73..101
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 170..174
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 184..190
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 214..218
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 227..231
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 264..267
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 292..296
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 306..317
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 318..322
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 335..343
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 344..347
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 367..373
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 384..387
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 389..397
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 398..406
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 462..467
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 468..475
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 478..486
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 507..511
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 523..533
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 553..558
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 560..562
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6TQF"
FT HELIX 587..596
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:6TQF"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 615..621
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 623..625
FT /evidence="ECO:0007829|PDB:6TQF"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:6TQF"
SQ SEQUENCE 639 AA; 71317 MW; DE85BBEEF42759A2 CRC64;
MGPKLFKPSI DWSRAFPDSV YWVGKAWTIS AICVLAILVL LRYLTPWGRQ FWRITRAYFV
GPNSVRVWLM LGVLLLSVVL AVRLNVLFSY QGNDMYTALQ KAFEGIASGD GTVKRSGVRG
FWMSIGVFSV MAVLHVTRVM ADIYLTQRFI IAWRVWLTHH LTQDWLDGRA YYRDLFIDET
IDNPDQRIQQ DVDIFTAGAG GTPNAPSNGT ASTLLFGAVQ SIISVISFTA ILWNLSGTLN
IFGVSIPRAM FWTVLVYVFV ATVISFIIGR PLIWLSFRNE KLNAAFRYAL VRLRDAAEAV
GFYRGERVEG TQLQRRFTPV IDNYRRYVRR SIAFNGWNLS VSQTIVPLPW VIQAPRLFAG
QIDFGDVGQT ATSFGNIHDS LSFFRNNYDA FASFRAAIIR LHGLVDANEK GRALPAVLTR
PSDDESVELN DIEVRTPAGD RLIDPLDVRL DRGGSLVITG RSGAGKTTLL RSLAELWPYA
SGTLHRPGGE NETMFLSQLP YVPLGTLRDV VCYPNSAAAI PDATLRDTLT KVALAPLCDR
LDEERDWAKV LSPGEQQRVA FARILLTKPK AVFLDESTSA LDTGLEFALY QLLRSELPDC
IVISVSHRPA LERLHENQLE LLGGGQWRLA PVEAAPAEV
