MPTA_MYCTU
ID MPTA_MYCTU Reviewed; 516 AA.
AC O53508; F2GJZ8; L0TBQ4;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Alpha-(1->6)-mannopyranosyltransferase A;
DE Short=MptA;
DE EC=2.4.1.-;
DE AltName: Full=Polyprenyl-1-monophosphorylmannose dependent alpha-(1->6)-mannopyranosyltransferase;
DE Short=PPM-dependent alpha-(1->6)-mannopyranosyltransferase;
GN Name=mptA; OrderedLocusNames=Rv2174;
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.
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).
RN [3]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 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 -!- SIMILARITY: Belongs to the MptA/B family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44951.1; -; Genomic_DNA.
DR PIR; H70935; H70935.
DR RefSeq; NP_216690.1; NC_000962.3.
DR AlphaFoldDB; O53508; -.
DR STRING; 83332.Rv2174; -.
DR iPTMnet; O53508; -.
DR PaxDb; O53508; -.
DR DNASU; 887528; -.
DR GeneID; 887528; -.
DR KEGG; mtu:Rv2174; -.
DR TubercuList; Rv2174; -.
DR eggNOG; ENOG502Z9GU; Bacteria.
DR OMA; TTVHPWY; -.
DR PhylomeDB; O53508; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:MTBBASE.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR InterPro; IPR017822; Carotene_biosyn-assoc_mem-1.
DR TIGRFAMs; TIGR03459; crt_membr; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..516
FT /note="Alpha-(1->6)-mannopyranosyltransferase A"
FT /id="PRO_0000420592"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:21969609"
SQ SEQUENCE 516 AA; 55294 MW; 1B78996B32BB60DD CRC64;
MTTPSHAPAV DLATAKDAVV QHLSRLFEFT TGPQGGPARL GFAGAVLITA GGLGAGSVRQ
HDPLLESIHM SWLRFGHGLV LSSILLWTGV GVMLLAWLGL GRRVLAGEAT EFTMRATTVI
WLAPLLLSVP VFSRDTYSYL AQGALLRDGL DPYAVGPVGN PNALLDDVSP IWTITTAPYG
PAFILVAKFV TVIVGNNVVA GTMLLRLCML PGLALLVWAT PRLASHLGTH GPTALWICVL
NPLVLIHLMG GVHNEMLMVG LMTAGIALTV QGRNVAGIIL ITVAIAVKAT AGIALPFLVW
VWLRHLRERR GYRPVQAFLA AAAISLLIFV AVFAVLSAVA GVGLGWLTAL AGSVKIINWL
TVPTGAANVI HALGRGLFTV DFYTLLRITR LIGIVIIAVS LPLLWWRFRR DDRAALTGVA
WSMLIVVLFV PAALPWYYSW PLAVAAPLAQ ARRAIAAIAG LSTWVMVIFK PDGSHGMYSW
LHFWIATACA LTAWYVLYRS PDRRGVQAAT PVVNTP
