AGBR_MYCTU
ID AGBR_MYCTU Reviewed; 121 AA.
AC P9WMS9; 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 35.
DE RecName: Full=Arabinogalactan biosynthesis recruiting protein Rv3789 {ECO:0000305|PubMed:26369580};
GN OrderedLocusNames=Rv3789; ORFNames=MTCY13D12.23;
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 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).
RN [3]
RP ORIGINAL FUNCTION AS A TRANSLOCASE, AND INTERACTION WITH GLFT1.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=23038254; DOI=10.1074/jbc.m112.400986;
RA Larrouy-Maumus G., Skovierova H., Dhouib R., Angala S.K., Zuberogoitia S.,
RA Pham H., Villela A.D., Mikusova K., Noguera A., Gilleron M.,
RA Valentinova L., Kordulakova J., Brennan P.J., Puzo G., Nigou J.,
RA Jackson M.;
RT "A small multidrug resistance-like transporter involved in the
RT arabinosylation of arabinogalactan and lipoarabinomannan in mycobacteria.";
RL J. Biol. Chem. 287:39933-39941(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=25906160; DOI=10.1021/acschembio.5b00237;
RA Brecik M., Centarova I., Mukherjee R., Kolly G.S., Huszar S., Bobovska A.,
RA Kilacskova E., Mokosova V., Svetlikova Z., Sarkan M., Neres J.,
RA Kordulakova J., Cole S.T., Mikusova K.;
RT "DprE1 is a vulnerable tuberculosis drug target due to its cell wall
RT localization.";
RL ACS Chem. Biol. 10:1631-1636(2015).
RN [5]
RP FUNCTION IN ARABINAN BIOSYNTHESIS, INDUCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, PATHWAY, INTERACTION WITH AFTA, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=26369580; DOI=10.1128/jb.00628-15;
RA Kolly G.S., Mukherjee R., Kilacskova E., Abriata L.A., Raccaud M.,
RA Blasko J., Sala C., Dal Peraro M., Mikusova K., Cole S.T.;
RT "GtrA protein Rv3789 is required for arabinosylation of arabinogalactan in
RT Mycobacterium tuberculosis.";
RL J. Bacteriol. 197:3686-3697(2015).
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:0000269|PubMed:26369580}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:26369580}.
CC -!- SUBUNIT: Interacts with the priming arabinosyltransferase AftA
CC (PubMed:26369580). Also interacts with the galactosyltransferase GlfT1,
CC which initiates the polymerization of the galactan domain of AG
CC (PubMed:23038254). Is thus probably part of an AG biosynthetic complex
CC (PubMed:23038254, PubMed:26369580). {ECO:0000269|PubMed:23038254,
CC ECO:0000269|PubMed:26369580}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:25906160,
CC ECO:0000269|PubMed:26369580}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000305|PubMed:26369580}.
CC -!- INDUCTION: Is cotranscribed with dprE1, dprE2 and aftA.
CC {ECO:0000269|PubMed:26369580}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display impaired growth
CC and abnormal cell morphology, since they are shorter and more swollen
CC than wild-type cells. This phenotype likely stems from the decreased
CC incorporation of arabinose into arabinogalactan observed in the
CC disruption mutant. The mutant also accumulates decaprenyl-phospho-
CC arabinose (DPA), the arabinose donor required for the synthesis of
CC cell-wall arabinans. The lipoglycan fraction comprising LAM
CC (lipoarabinomannan) and LM (lipomannan) is not affected.
CC {ECO:0000269|PubMed:26369580}.
CC -!- SIMILARITY: Belongs to the GtrA family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a lipid-linked sugar translocase
CC involved in the reorientation and export of decaprenyl-phospho-
CC arabinose (DPA) across the plasma membrane to the site of AG
CC (arabinogalactan) and LAM (lipoarabinomannan) synthesis
CC (PubMed:23038254). It was later shown that synthesis of DPA takes place
CC in the periplasm and it was suggested that Rv3789 does not act as a DPA
CC flippase but, rather, recruits AftA for arabinogalactan biosynthesis
CC (PubMed:25906160, PubMed:26369580). {ECO:0000305|PubMed:23038254,
CC ECO:0000305|PubMed:25906160, ECO:0000305|PubMed:26369580}.
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DR EMBL; AL123456; CCP46618.1; -; Genomic_DNA.
DR PIR; A70697; A70697.
DR RefSeq; NP_218306.1; NC_000962.3.
DR RefSeq; WP_003420627.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; P9WMS9; -.
DR STRING; 83332.Rv3789; -.
DR TCDB; 2.A.129.1.2; the lipid-linked sugar translocase (lst) family.
DR PaxDb; P9WMS9; -.
DR DNASU; 886109; -.
DR GeneID; 886109; -.
DR KEGG; mtu:Rv3789; -.
DR PATRIC; fig|83332.111.peg.4213; -.
DR TubercuList; Rv3789; -.
DR eggNOG; COG2246; Bacteria.
DR OMA; WTFQAAP; -.
DR PhylomeDB; P9WMS9; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..121
FT /note="Arabinogalactan biosynthesis recruiting protein
FT Rv3789"
FT /id="PRO_0000212257"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26369580"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..26
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:26369580"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:26369580"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..91
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:26369580"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 113..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:26369580"
SQ SEQUENCE 121 AA; 13377 MW; D62028BE43EA0FE8 CRC64;
MRFVVTGGLA GIVDFGLYVV LYKVAGLQVD LSKAISFIVG TITAYLINRR WTFQAEPSTA
RFVAVMLLYG ITFAVQVGLN HLCLALLHYR AWAIPVAFVI AQGTATVINF IVQRAVIFRI
R
