ID   AGBR_MYCBO              Reviewed;         121 AA.
AC   P64293; A0A1R3Y5A1; P72055; X2BPU5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Arabinogalactan biosynthesis recruiting protein Mb3818;
GN   OrderedLocusNames=BQ2027_MB3818;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02447.1; -; Genomic_DNA.
DR   RefSeq; NP_857455.1; NC_002945.3.
DR   RefSeq; WP_003420627.1; NC_002945.4.
DR   AlphaFoldDB; P64293; -.
DR   EnsemblBacteria; SIU02447; SIU02447; BQ2027_MB3818.
DR   PATRIC; fig|233413.5.peg.4175; -.
DR   OMA; WTFQAAP; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000001419; 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                   Mb3818"
FT                   /id="PRO_0000212258"
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