AFTB_CORGL
ID AFTB_CORGL Reviewed; 686 AA.
AC Q8NLR0; Q6M1Y1;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Terminal beta-(1->2)-arabinofuranosyltransferase;
DE EC=2.4.2.-;
GN Name=aftB; OrderedLocusNames=Cgl2879, cg3187;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [3]
RP FUNCTION, DISRUPTION PHENOTYPE, 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).
CC -!- FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG)
CC region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC essential component of the cell wall. Catalyzes the transfer of
CC arabinofuranosyl (Araf) residues from the sugar donor decaprenyl-
CC phospho-arabinose (DPA) to the arabinan domain to form terminal beta-
CC (1->2)-linked Araf residues, which marks the end point for AG arabinan
CC 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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene show an absence of the
CC cell wall-bound corynomycolic acids and of beta-(1->2) Araf linkage.
CC {ECO:0000269|PubMed:17387176}.
CC -!- SIMILARITY: Belongs to the AftB family. {ECO:0000305}.
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DR EMBL; BA000036; BAC00273.1; -; Genomic_DNA.
DR EMBL; BX927156; CAF20903.1; -; Genomic_DNA.
DR RefSeq; NP_602070.1; NC_003450.3.
DR AlphaFoldDB; Q8NLR0; -.
DR STRING; 196627.cg3187; -.
DR CAZy; GT89; Glycosyltransferase Family 89.
DR KEGG; cgb:cg3187; -.
DR KEGG; cgl:Cgl2879; -.
DR PATRIC; fig|196627.13.peg.2811; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_423257_0_0_11; -.
DR OMA; MGDDATH; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000582; 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 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..686
FT /note="Terminal beta-(1->2)-arabinofuranosyltransferase"
FT /id="PRO_0000420578"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 351
FT /note="L -> V (in Ref. 2; CAF20903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 75840 MW; 6117C0D69033F482 CRC64;
MTFSPQRPEF ETGKQPDPET EHAGDFFEET SSSAPRAASN GSSGPNYTLI TTFLAALTAG
IFAFWAGWTR KWISDDGLIV LRTVRNLLAG NGPVFNAGER VEANTSTLWQ YCIYLVALVT
DYRLEDIALW LALLFTTAAS IIGVLGTAHL HRKRIAVLLP AGVIGYFSLS PARDFATSGL
EWGLSLMWIS IQWLLLVLWA TSGKTSGKKA SGAKTSNPIV NAGAITYALA FWSGLSWLVR
PELAMYGGLT GVLLLLTAPR WRVVLGILVA ALPLPAAYQI FRMGYYGLMV PHTAVAKSAS
DAVWGTGWEY VEDFTGPYNL WLGLALLLAA GALTVWKTDK HLAIPKGRLG LRTPGMAIAL
LVICALVHFL YVIRVGGDFM HGRMLLLPLF AILLPVSVIP VNVVDRGWQD LVALVLVFST
WVWSTVVFVQ GHQWENTGQH VVDERDFWID FTNRDEDHPP LYAEDFLTVD SMNDYAEVMR
DQTLVNPTGQ QLNILASSDP TTYSWITTPR VEGVEAGDLA NLSPTVFHVN LGMTSMNAPL
NVRVTDLIGL ATPLAARQPR IEGGRIGHDK LMDLEWQVAE SATPLAYTPG WLDTQKTYEA
RQALRHPELV HLFQTYREPM SYHRFVDNIK YALTTGRTLE ISDNPEDLLK EFNPTPAEIQ
DGLETIAWPG EIKLDEPRGE PLYSSQ
