ID   AGBR_MYCTO              Reviewed;         121 AA.
AC   P9WMS8; L0TDJ8; P64292; P72055;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Arabinogalactan biosynthesis recruiting protein MT3897;
GN   OrderedLocusNames=MT3897;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; 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: 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK48262.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK48262.1; ALT_INIT; Genomic_DNA.
DR   PIR; A70697; A70697.
DR   RefSeq; WP_003420627.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMS8; -.
DR   EnsemblBacteria; AAK48262; AAK48262; MT3897.
DR   KEGG; mtc:MT3897; -.
DR   PATRIC; fig|83331.31.peg.4192; -.
DR   HOGENOM; CLU_083873_3_1_11; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000001020; 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; Transmembrane; Transmembrane helix.
FT   CHAIN           1..121
FT                   /note="Arabinogalactan biosynthesis recruiting protein
FT                   MT3897"
FT                   /id="PRO_0000427249"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..26
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..61
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        83..91
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P9WMS9"
SQ   SEQUENCE   121 AA;  13377 MW;  D62028BE43EA0FE8 CRC64;
     MRFVVTGGLA GIVDFGLYVV LYKVAGLQVD LSKAISFIVG TITAYLINRR WTFQAEPSTA
     RFVAVMLLYG ITFAVQVGLN HLCLALLHYR AWAIPVAFVI AQGTATVINF IVQRAVIFRI
     R