PAPA1_MYCBO
ID PAPA1_MYCBO Reviewed; 511 AA.
AC Q7TVK9; A0A1R3Y5E3; X2BQ32;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=2'-acyl-2-O-sulfo-trehalose (hydroxy)phthioceranyltransferase PapA1 {ECO:0000250|UniProtKB:P9WIK9};
DE EC=2.3.1.283 {ECO:0000250|UniProtKB:P9WIK9};
DE AltName: Full=Polyketide synthase-associated protein A1;
DE AltName: Full=SL659 acyltransferase PapA1 {ECO:0000250|UniProtKB:P9WIK9};
GN Name=papA1; OrderedLocusNames=BQ2027_MB3854C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Required for the biosynthesis of sulfolipid-1 (SL-1), a major
CC mycobacterial cell wall lipid. Catalyzes the acylation of trehalose-2-
CC sulfate-2'-palmitate (SL659) by adding the (hydroxy)phthioceranoyl
CC group at the 3'-position to yield the diacylated intermediate 2-
CC palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D-trehalose-2'-sulfate
CC (SL1278). {ECO:0000250|UniProtKB:P9WIK9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (hydroxy)phthioceranyl-[(hydroxy)phthioceranic acid
CC synthase] + 2'-palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose = a
CC 3'-(hydroxy)phthioceranyl-2'-palmitoyl/stearoyl-2-O-sulfo-
CC alpha,alpha-trehalose + holo-[(hydroxy)phthioceranic acid synthase].;
CC EC=2.3.1.283; Evidence={ECO:0000250|UniProtKB:P9WIK9};
CC -!- SIMILARITY: Belongs to the PapA acyltransferase family. {ECO:0000305}.
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DR EMBL; LT708304; SIU02483.1; -; Genomic_DNA.
DR RefSeq; NP_857491.1; NC_002945.3.
DR RefSeq; WP_003899711.1; NC_002945.4.
DR AlphaFoldDB; Q7TVK9; -.
DR SMR; Q7TVK9; -.
DR EnsemblBacteria; SIU02483; SIU02483; BQ2027_MB3854C.
DR PATRIC; fig|233413.5.peg.4215; -.
DR OMA; AEIHLMY; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR Pfam; PF00668; Condensation; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell wall biogenesis/degradation; Lipid biosynthesis;
KW Lipid metabolism; Transferase.
FT CHAIN 1..511
FT /note="2'-acyl-2-O-sulfo-trehalose
FT (hydroxy)phthioceranyltransferase PapA1"
FT /id="PRO_0000314656"
SQ SEQUENCE 511 AA; 56128 MW; 07D7766EF181C4E5 CRC64;
MRIGPVELSA VKDWDPAPGV LVSWHPTPAS CAKALAAPVS AVPPSYVQAR QIRSFSEQAA
RGLDHSRLLI ASVEVFGHCD LRAMTYVINA HLRRHDTYRS WFELRDTDHI VRHSIADPAD
IEFVPTTHGE MTSADLRQHI VATPDSLHWD CFSFGVIQRA DSFTFYASID HLHADGQFVG
VGLMEFQSMY TALIMGEPPI GLSEAGSYVD FCVRQHEYTS ALTVDSPEVR AWIDFAEINN
GTFPEFPLPL GDPSVRCGGD LLSMMLMDEQ QTQRFESACM AANARFIGGM LACIAIAIHE
LTGADTYFGI TPKDIRTPAD LMTQGWFTGQ IPVTVPVAGL SFNEIARIAQ TSFDTGADLA
KVPFERVVEL SPSLRRPQPL FSLVNFFDAQ VGPLSAVTKL FEGLNVGTYS DGRVTYPLST
MVGRFDETAA SVLFPDNPVA RESVTAYLRA IRSVCMRIAN GGTAERVGNV VALSPGRRNN
IERMTWRSCR AGDFIDICNL KVANVTVDRE A