MPTA_CORGL
ID MPTA_CORGL Reviewed; 490 AA.
AC Q8NNM0; Q6M3R0;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Alpha-(1->6)-mannopyranosyltransferase A;
DE Short=MptA;
DE EC=2.4.1.-;
GN Name=mptA; OrderedLocusNames=Cgl2173, cg2385;
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=17714444; DOI=10.1111/j.1365-2958.2007.05884.x;
RA Mishra A.K., Alderwick L.J., Rittmann D., Tatituri R.V., Nigou J.,
RA Gilleron M., Eggeling L., Besra G.S.;
RT "Identification of an alpha(1-->6) mannopyranosyltransferase (MptA),
RT involved in Corynebacterium glutamicum lipomanann biosynthesis, and
RT identification of its orthologue in Mycobacterium tuberculosis.";
RL Mol. Microbiol. 65:1503-1517(2007).
CC -!- FUNCTION: Involved in the latter stages of the biosynthesis of the
CC alpha-(1->6) mannan core of lipomannan (LM). Catalyzes the addition of
CC alpha-(1->6)-mannose residue. {ECO:0000269|PubMed:17714444}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a complete loss of
CC LM biosynthesis. Mutant results in the formation of a truncated LM with
CC a reduction of alpha-(1->6) and alpha-(1->2) glycosidic linkages.
CC {ECO:0000269|PubMed:17714444}.
CC -!- SIMILARITY: Belongs to the MptA/B family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF20514.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000036; BAB99566.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20514.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_601377.1; NC_003450.3.
DR AlphaFoldDB; Q8NNM0; -.
DR STRING; 196627.cg2385; -.
DR KEGG; cgb:cg2385; -.
DR KEGG; cgl:Cgl2173; -.
DR PATRIC; fig|196627.13.peg.2110; -.
DR eggNOG; ENOG502Z9GU; Bacteria.
DR HOGENOM; CLU_023913_1_0_11; -.
DR OMA; TTVHPWY; -.
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 InterPro; IPR017822; Carotene_biosyn-assoc_mem-1.
DR TIGRFAMs; TIGR03459; crt_membr; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..490
FT /note="Alpha-(1->6)-mannopyranosyltransferase A"
FT /id="PRO_0000420591"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 52307 MW; 32B7CD7F38115031 CRC64;
MLLLGSFGGG AIRYRGGVLD ALGLNFLAFG HAQGISNTVL WVGQLLLIGA WVHLGRRLFK
KKVADDTADA ADLGLVKRTL YAMVVPLIFA APMMSRDVYS YLMQGAMLRD GFDPYTEGAA
VNPGPMLLEV SHDWRNTTTP YGPLHLWIGD MITTVVGDNV TLGVVAYKIL SIIGLAVTGW
SIVRIAQHFG ANPAIALWIG VANPVMIIHM IGGMHNESLM VGLVSVGLLL ALKKRFVAGV
ALIAVAVSLK ATAAIALPFV VWIGMHHFAG FLATKKGKDS PTLKQQVPAF FATGAAGVAV
TGVVVSAITW ASGASWGWIS EISGNSKVIN PLAFPSLVAS VITMVAEVFV DDFDYNAVVN
VVRSISMLIM LGGLVVCWWL FRQNERRAVT GTAAAYAVAF VFNSVTLPWY YASLISLLGT
FKPPMWLIRF AAGASVFIAL MFTGSGNHQL YNIVTVIIAA IIAWLATVVI FDDTDPATTA
TEKPSPHTVS
