ABC1_MYCTU
ID ABC1_MYCTU Reviewed; 865 AA.
AC O65934; F2GJI0; L0TAH8;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=ABC transporter ATP-binding/permease protein Rv1747;
DE EC=7.-.-.-;
GN OrderedLocusNames=Rv1747;
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, ATPASE ACTIVITY, SUBUNIT, DOMAIN, PHOSPHORYLATION BY PKNF, AND
RP MUTAGENESIS OF ARG-33; SER-47; ASN-69; ARG-234; SER-248; ASN-270 AND
RP GLU-479.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15135525; DOI=10.1111/j.1574-6968.2004.tb09536.x;
RA Molle V., Soulat D., Jault J.M., Grangeasse C., Cozzone A.J., Prost J.F.;
RT "Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation
RT by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis.";
RL FEMS Microbiol. Lett. 234:215-223(2004).
RN [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH PKNF, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF SER-47 AND SER-248.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16040957; DOI=10.1128/iai.73.8.4471-4477.2005;
RA Curry J.M., Whalan R., Hunt D.M., Gohil K., Strom M., Rickman L.,
RA Colston M.J., Smerdon S.J., Buxton R.S.;
RT "An ABC transporter containing a forkhead-associated domain interacts with
RT a serine-threonine protein kinase and is required for growth of
RT Mycobacterium tuberculosis in mice.";
RL Infect. Immun. 73:4471-4477(2005).
RN [4]
RP PHOSPHORYLATION.
RX PubMed=15987910; DOI=10.1110/ps.051413405;
RA Grundner C., Gay L.M., Alber T.;
RT "Mycobacterium tuberculosis serine/threonine kinases PknB, PknD, PknE, and
RT PknF phosphorylate multiple FHA domains.";
RL Protein Sci. 14:1918-1921(2005).
RN [5]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT THR-152 AND THR-210, AND
RP MUTAGENESIS OF SER-47; THR-152; THR-210 AND SER-248.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21622570; DOI=10.1074/jbc.m111.246132;
RA Spivey V.L., Molle V., Whalan R.H., Rodgers A., Leiba J., Stach L.,
RA Walker K.B., Smerdon S.J., Buxton R.S.;
RT "Forkhead-associated (FHA) domain containing ABC transporter Rv1747 is
RT positively regulated by Ser/Thr phosphorylation in Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 286:26198-26209(2011).
RN [6]
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: Involved in the translocation of an unknown substrate across
CC the membrane. Transmembrane domains (TMD) form a pore in the membrane
CC and the ATP-binding domain (NBD) is responsible for energy generation.
CC Required for virulence. {ECO:0000269|PubMed:15135525,
CC ECO:0000269|PubMed:16040957}.
CC -!- ACTIVITY REGULATION: Function is positively regulated by
CC phosphorylation. {ECO:0000269|PubMed:21622570}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with PknF.
CC {ECO:0000269|PubMed:15135525, ECO:0000269|PubMed:16040957,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: In Rv1747 the ATP-binding domain (NBD) and the transmembrane
CC domain (TMD) are fused. The two FHA domains are required for
CC phosphorylation by PknF. {ECO:0000269|PubMed:15135525}.
CC -!- PTM: Phosphorylated by PknF. Can probably be phosphorylated in vivo by
CC other kinases when PknF is missing. {ECO:0000269|PubMed:15135525,
CC ECO:0000269|PubMed:15987910, ECO:0000269|PubMed:21622570}.
CC -!- DISRUPTION PHENOTYPE: Disruption results in a growth defect in
CC macrophage and mouse infections. {ECO:0000269|PubMed:16040957}.
CC -!- SIMILARITY: In the central section; belongs to the ABC transporter
CC superfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ABC-2 integral
CC membrane protein family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44513.1; -; Genomic_DNA.
DR PIR; D70986; D70986.
DR RefSeq; NP_216263.1; NC_000962.3.
DR RefSeq; WP_003408545.1; NZ_NVQJ01000010.1.
DR PDB; 6CAH; NMR; -; A=207-310.
DR PDB; 6CCD; X-ray; 1.80 A; A=3-113.
DR PDBsum; 6CAH; -.
DR PDBsum; 6CCD; -.
DR AlphaFoldDB; O65934; -.
DR SMR; O65934; -.
DR STRING; 83332.Rv1747; -.
DR iPTMnet; O65934; -.
DR PaxDb; O65934; -.
DR DNASU; 885311; -.
DR GeneID; 45425720; -.
DR GeneID; 885311; -.
DR KEGG; mtu:Rv1747; -.
DR TubercuList; Rv1747; -.
DR eggNOG; COG0842; Bacteria.
DR eggNOG; COG1131; Bacteria.
DR eggNOG; COG1716; Bacteria.
DR InParanoid; O65934; -.
DR OMA; RWSIGAY; -.
DR PhylomeDB; O65934; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd00060; FHA; 2.
DR DisProt; DP01947; -.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF00498; FHA; 2.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00240; FHA; 2.
DR SUPFAM; SSF49879; SSF49879; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..865
FT /note="ABC transporter ATP-binding/permease protein Rv1747"
FT /id="PRO_0000419321"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 29..78
FT /note="FHA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 230..279
FT /note="FHA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT DOMAIN 319..552
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 596..810
FT /note="ABC transmembrane type-2"
FT REGION 104..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21622570"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:21622570"
FT MUTAGEN 33
FT /note="R->A: Strong decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:15135525"
FT MUTAGEN 47
FT /note="S->A: Strong decrease in phosphorylation. Lack of
FT interaction with PknF. Attenuates growth in macrophages."
FT /evidence="ECO:0000269|PubMed:15135525,
FT ECO:0000269|PubMed:16040957, ECO:0000269|PubMed:21622570"
FT MUTAGEN 69
FT /note="N->A: Strong decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:15135525"
FT MUTAGEN 152
FT /note="T->A: Lack of phosphorylation. Attenuates growth in
FT macrophages and in mice; when associated with A-210."
FT /evidence="ECO:0000269|PubMed:21622570"
FT MUTAGEN 210
FT /note="T->A: Lack of phosphorylation. Attenuates growth in
FT macrophages and in mice; when associated with A-152."
FT /evidence="ECO:0000269|PubMed:21622570"
FT MUTAGEN 234
FT /note="R->A: Strong decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:15135525"
FT MUTAGEN 248
FT /note="S->A: Strong decrease in phosphorylation. Decreases
FT interaction with PknF."
FT /evidence="ECO:0000269|PubMed:15135525,
FT ECO:0000269|PubMed:16040957, ECO:0000269|PubMed:21622570"
FT MUTAGEN 270
FT /note="N->A: Strong decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:15135525"
FT MUTAGEN 479
FT /note="E->Q: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:15135525"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 79..93
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:6CCD"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:6CAH"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6CAH"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:6CAH"
SQ SEQUENCE 865 AA; 92153 MW; 4987186C471E47E8 CRC64;
MPMSQPAAPP VLTVRYEGSE RTFAAGHDVV VGRDLRADVR VAHPLISRAH LLLRFDQGRW
VAIDNGSLNG LYLNNRRVPV VDIYDAQRVH IGNPDGPALD FEVGRHRGSA GRPPQTTSIR
LPNLSAGAWP TDGPPQTGTL GSGQLQQLPP ATTRIPAAPP SGPQPRYPTG GQQLWPPSGP
QRAPQIYRPP TAAPPPAGAR GGTEAGNLAT SMMKILRPGR LTGELPPGAV RIGRANDNDI
VIPEVLASRH HATLVPTPGG TEIRDNRSIN GTFVNGARVD AALLHDGDVV TIGNIDLVFA
DGTLARREEN LLETRVGGLD VRGVTWTIDG DKTLLDGISL TARPGMLTAV IGPSGAGKST
LARLVAGYTH PTDGTVTFEG HNVHAEYASL RSRIGMVPQD DVVHGQLTVK HALMYAAELR
LPPDTTKDDR TQVVARVLEE LEMSKHIDTR VDKLSGGQRK RASVALELLT GPSLLILDEP
TSGLDPALDR QVMTMLRQLA DAGRVVLVVT HSLTYLDVCD QVLLLAPGGK TAFCGPPTQI
GPVMGTTNWA DIFSTVADDP DAAKARYLAR TGPTPPPPPV EQPAELGDPA HTSLFRQFST
IARRQLRLIV SDRGYFVFLA LLPFIMGALS MSVPGDVGFG FPNPMGDAPN EPGQILVLLN
VGAVFMGTAL TIRDLIGERA IFRREQAVGL STTAYLIAKV CVYTVLAVVQ SAIVTVIVLV
GKGGPTQGAV ALSKPDLELF VDVAVTCVAS AMLGLALSAI AKSNEQIMPL LVVAVMSQLV
FSGGMIPVTG RVPLDQMSWV TPARWGFAAS AATVDLIKLV PGPLTPKDSH WHHTASAWWF
DMAMLVALSV IYVGFVRWKI RLKAC
