ID   AGBR_MYCLE              Reviewed;         123 AA.
AC   Q9CDA3;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Arabinogalactan biosynthesis recruiting protein ML0110;
GN   OrderedLocusNames=ML0110;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Required for arabinosylation of arabinogalactan (AG), an
CC       essential component of the mycobacterial cell wall. Probably acts as an
CC       anchor protein recruiting AftA, the first arabinosyl transferase
CC       involved in AG biosynthesis. {ECO:0000250|UniProtKB:P9WMS9}.
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC       {ECO:0000250|UniProtKB:P9WMS9}.
CC   -!- SUBUNIT: Interacts with the priming arabinosyltransferase AftA.
CC       {ECO:0000250|UniProtKB:P9WMS9}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P9WMS9}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P9WMS9, ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the GtrA family. {ECO:0000305}.
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DR   EMBL; AL583917; CAC29618.1; -; Genomic_DNA.
DR   PIR; F86922; F86922.
DR   RefSeq; NP_301207.1; NC_002677.1.
DR   RefSeq; WP_010907532.1; NC_002677.1.
DR   AlphaFoldDB; Q9CDA3; -.
DR   SMR; Q9CDA3; -.
DR   STRING; 272631.ML0110; -.
DR   EnsemblBacteria; CAC29618; CAC29618; CAC29618.
DR   KEGG; mle:ML0110; -.
DR   PATRIC; fig|272631.5.peg.173; -.
DR   Leproma; ML0110; -.
DR   eggNOG; COG2246; Bacteria.
DR   HOGENOM; CLU_083873_3_1_11; -.
DR   OMA; VITMATY; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   InterPro; IPR007267; GtrA.
DR   Pfam; PF04138; GtrA; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..123
FT                   /note="Arabinogalactan biosynthesis recruiting protein
FT                   ML0110"
FT                   /id="PRO_0000212259"
FT   TOPO_DOM        1
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        23..27
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..67
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..93
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..123
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
SQ   SEQUENCE   123 AA;  13861 MW;  B01DDB9E30AC52B0 CRC64;
     MLRFIVTGSL ATAVDFSVYV TLYRGGGLQV DLAKFTSVVI GTITSYMINR RWTFQMSPST
     TRFAAVMALY GITFAVQMGL NHLCLFLFHY QEPWAIPIAF VIAQGLATVI NFIVQRVVIF
     RIR