ID BACA_MYCTO Reviewed; 639 AA.
AC P9WQI8; L0TAH3; Q50614;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Hydrophilic compounds import ATP-binding/permease protein BacA {ECO:0000250|UniProtKB:P9WQI9};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:P9WQI9};
DE AltName: Full=Hydrophilic compounds ABC transporter BacA {ECO:0000250|UniProtKB:P9WQI9};
GN Name=bacA; OrderedLocusNames=MT1867;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Multi-solute ABC transporter that mediates uptake of
CC unrelated hydrophilic compounds. Can transport vitamin B12 and related
CC corrinoids, and antimicrobial peptides such as bleomycin. Transmembrane
CC domains (TMD) form a pore in the membrane and the ATP-binding domain
CC (NBD) is responsible for energy generation.
CC {ECO:0000250|UniProtKB:P9WQI9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WQI9}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WQI9};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P9WQI9}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; AE000516; AAK46140.1; -; Genomic_DNA.
DR PIR; D70720; D70720.
DR RefSeq; WP_003900416.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WQI8; -.
DR SMR; P9WQI8; -.
DR KEGG; mtc:MT1867; -.
DR PATRIC; fig|83331.31.peg.2010; -.
DR HOGENOM; CLU_007587_6_2_11; -.
DR Proteomes; UP000001020; Chromosome.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03223; ABCD_peroxisomal_ALDP; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR11384:SF59; ATP-BINDING CASSETTE SUB-FAMILY D MEMBER; 1.
DR PANTHER; PTHR11384; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1.
DR Pfam; PF06472; ABC_membrane_2; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW 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_0000426768"
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:0000250|UniProtKB:P9WQI9"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P9WQI9"
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
//
