AFTC_CORGL
ID AFTC_CORGL Reviewed; 418 AA.
AC Q8NPB7; Q6M4C2;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Alpha-(1->3)-arabinofuranosyltransferase {ECO:0000303|PubMed:18627460};
DE EC=2.4.2.47 {ECO:0000250|UniProtKB:A0QW28};
DE AltName: Full=Arabinofuranan 3-O-arabinosyltransferase {ECO:0000305|PubMed:18627460};
DE AltName: Full=Arabinofuranosyltransferase C;
GN Name=aftC {ECO:0000303|PubMed:18627460};
GN OrderedLocusNames=Cgl1897 {ECO:0000312|EMBL:BAB99290.1};
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 FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=18627460; DOI=10.1111/j.1365-2958.2008.06354.x;
RA Birch H.L., Alderwick L.J., Bhatt A., Rittmann D., Krumbach K., Singh A.,
RA Bai Y., Lowary T.L., Eggeling L., Besra G.S.;
RT "Biosynthesis of mycobacterial arabinogalactan: identification of a novel
RT alpha(1-->3) arabinofuranosyltransferase.";
RL Mol. Microbiol. 69:1191-1206(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG)
CC region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC essential component of the corynebacterial cell wall. Catalyzes the
CC addition of an arabinofuranosyl (Araf) residue from the sugar donor
CC beta-D-arabinofuranosyl-1-monophosphoryldecaprenol (DPA) on the C-3 of
CC an alpha-(1->5)-linked Araf from the arabinan backbone of AG.
CC {ECO:0000269|PubMed:18627460}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Adds an alpha-D-arabinofuranosyl group from trans,octacis-
CC decaprenylphospho-beta-D-arabinofuranose at the 3-O-position of an
CC alpha-(1->5)-arabinofuranan chain attached to a beta-(1->5)-
CC galactofuranan chain.; EC=2.4.2.47;
CC Evidence={ECO:0000250|UniProtKB:A0QW28};
CC -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:18627460}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show reduced levels of
CC cell wall-bound corynomycolic acid methyl esters (CMAMEs).
CC {ECO:0000269|PubMed:18627460}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 87 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000036; BAB99290.1; -; Genomic_DNA.
DR RefSeq; NP_601103.1; NC_003450.3.
DR AlphaFoldDB; Q8NPB7; -.
DR STRING; 196627.cg2077; -.
DR KEGG; cgl:Cgl1897; -.
DR PATRIC; fig|196627.13.peg.1834; -.
DR eggNOG; ENOG5033U55; Bacteria.
DR HOGENOM; CLU_055106_0_0_11; -.
DR OMA; AMFCTES; -.
DR UniPathway; UPA00963; -.
DR Proteomes; UP000000582; 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:0016758; F:hexosyltransferase activity; IEA:InterPro.
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; IPR018584; GT87.
DR Pfam; PF09594; GT87; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..418
FT /note="Alpha-(1->3)-arabinofuranosyltransferase"
FT /id="PRO_0000451751"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 418 AA; 46837 MW; DA1F4DC16E60A490 CRC64;
MSFSPVAPSI SAPTPRRSRW DSIGNAVAWP LAMLLMAHRF FVLAINGAVT DDFTTVYSAL
RRFVEGIPVY NEVYHFVDPH YLYNPGATLL LAPLGYITHF TLARWMFIAV NLLAIVLAFG
LLTRLSGWAL RSMVWPIAIA LAMLTETVQN TLIFSNINGI LLLMLAIFLW CVVHKKSWLG
GLVIGLAILI KPMFLPLLFL PLVKKQWGSL ILGILTPVIF NAVAWFLVPG ASEYVTRTMP
YLGETRDFAN SSLPGLAIYF GMPTWMEITW FLIFGAMVGL AVLALLRFRN TEPYFWAATT
TGVLLTGVFF LSSLGQMYYS MMIFPMIFTL LGSRSVFHNW VAWVAAYFFL SPDTFTSQRL
PDVARWMEFF SATVGWGLLI VVTFVSALIW FIGDIRAKGT PSSPITTDPT HDHLERTA
