AFTB_MYCTU
ID AFTB_MYCTU Reviewed; 627 AA.
AC O53582; F2GDG4; L0TDU7;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Terminal beta-(1->2)-arabinofuranosyltransferase;
DE EC=2.4.2.-;
DE Flags: Precursor;
GN Name=aftB; OrderedLocusNames=Rv3805c;
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, AND NOMENCLATURE.
RX PubMed=17387176; DOI=10.1074/jbc.m700271200;
RA Seidel M., Alderwick L.J., Birch H.L., Sahm H., Eggeling L., Besra G.S.;
RT "Identification of a novel arabinofuranosyltransferase AftB involved in a
RT terminal step of cell wall arabinan biosynthesis in Corynebacterianeae,
RT such as Corynebacterium glutamicum and Mycobacterium tuberculosis.";
RL J. Biol. Chem. 282:14729-14740(2007).
RN [3]
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 biosynthesis of the arabinogalactan (AG)
CC region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC essential component of the mycobacterial cell wall. Catalyzes the
CC transfer of arabinofuranosyl (Araf) residues from the sugar donor
CC decaprenyl-phospho-arabinose (DPA) to the arabinan domain to form
CC terminal beta-(1->2)-linked Araf residues, which marks the end point
CC for AG arabinan biosynthesis before decoration with mycolic acids.
CC {ECO:0000269|PubMed:17387176}.
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the AftB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46634.1; -; Genomic_DNA.
DR PIR; A70888; A70888.
DR RefSeq; NP_218322.1; NC_000962.3.
DR AlphaFoldDB; O53582; -.
DR STRING; 83332.Rv3805c; -.
DR PaxDb; O53582; -.
DR PRIDE; O53582; -.
DR DNASU; 886138; -.
DR GeneID; 886138; -.
DR KEGG; mtu:Rv3805c; -.
DR PATRIC; fig|83332.111.peg.4230; -.
DR TubercuList; Rv3805c; -.
DR eggNOG; COG1807; Bacteria.
DR InParanoid; O53582; -.
DR OMA; MGDDATH; -.
DR PhylomeDB; O53582; -.
DR BioCyc; MetaCyc:G185E-8101-MON; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..627
FT /note="Terminal beta-(1->2)-arabinofuranosyltransferase"
FT /id="PRO_0000420577"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 627 AA; 68710 MW; 8D4BB68854765EBA CRC64;
MVRVSLWLSV TAVAVLFGWG SWQRRWIADD GLIVLRTVRN LLAGNGPVFN QGERVEANTS
TAWTYLLYVG GWVGGPMRLE YVALALAMVL SLLGMVLLML GTGRLYAPSL RGRRAIMLPA
GALVYIAVPP ARDFATSGLE SGLVLAYLGL LWWMMVCWSQ PLRARPDSQM FLGALAFVAG
CSVLVRPEFA LIGGLALIMM LIAARTWRRR VLIVLAGGFL PVAYQIFRMG YYGLLVPSTA
LAKDAAGDKW SQGMIYVSNF NRPYALWVPL VLSVPLGLLL MTARRRPSFL RPVLAPDYGR
VARAVQSPPA VVAFIVGSGV LQALYWIRQG GDFMHGRVLL APLFCLLAPV GVIPILLPDG
KDFSRETGRW LVGALSGLWL GIAGWSLWAA NSPGMGDDAT RVTYSGIVDE RRFYAQATGH
AHPLTAADYL DYPRMAAVLT ALNNTPEGAL LLPSGNYNQW DLVPMIRPSS GTAPGGKPAP
KPQHAVFFTN MGMLGMNVGL DVRVIDQIGL VNPLAAHTER LKHARIGHDK NLFPDWVIAD
GPWVKWYPGI PGYIDQQWVT QAEAALQCPA TRAVLNSVRA PITLHRFLSN VLHSYEFTRY
RIDRVPRYEL VRCGLDVPDG PGPPPRE
