CHP1_MYCTU
ID CHP1_MYCTU Reviewed; 404 AA.
AC O07801; F2GDI1; I6Y4L6; L0TGP4;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=SL1278 acyltransferase Chp1 {ECO:0000305};
DE EC=2.3.1.284 {ECO:0000269|PubMed:22194604};
DE AltName: Full=Cutinase-like hydrolase protein {ECO:0000303|PubMed:22194604};
GN Name=chp1 {ECO:0000303|PubMed:22194604};
GN OrderedLocusNames=Rv3822 {ECO:0000312|EMBL:CCP46651.1},
GN RVBD_3822 {ECO:0000312|EMBL:AFN51848.1};
GN ORFNames=LH57_20830 {ECO:0000312|EMBL:AIR16616.1},
GN P425_03980 {ECO:0000312|EMBL:KBJ24899.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TOPOLOGY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-156.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=22194604; DOI=10.1074/jbc.m111.315473;
RA Seeliger J.C., Holsclaw C.M., Schelle M.W., Botyanszki Z., Gilmore S.A.,
RA Tully S.E., Niederweis M., Cravatt B.F., Leary J.A., Bertozzi C.R.;
RT "Elucidation and chemical modulation of sulfolipid-1 biosynthesis in
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 287:7990-8000(2012).
CC -!- FUNCTION: Involved in the final steps of the cell wall sulfolipid-1
CC (SL-1) biosynthesis. Catalyzes two successive acylations of the
CC precursor 2-palmitoyl-3-(C43)-phthioceranyl-alpha, alpha'-D-trehalose-
CC 2'-sulfate (SL1278) to yield the tetraacylated sulfolipid SL-1.
CC {ECO:0000269|PubMed:22194604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 3'-(hydroxy)phthioceranyl-2'-palmitoyl(stearoyl)-2-O-sulfo-
CC alpha,alpha-trehalose = 3,6,6'-tris-(hydroxy)phthioceranyl-2-
CC palmitoyl(stearoyl)-2'-sulfo-alpha-alpha-trehalose + 2 2'-
CC palmitoyl/stearoyl-2-O-sulfo-alpha,alpha-trehalose.; EC=2.3.1.284;
CC Evidence={ECO:0000269|PubMed:22194604};
CC -!- ACTIVITY REGULATION: Activity is potentiated by the SL-1 transporter
CC MmpL8. Inhibited by the lipase inhibitor tetrahydrolipstatin (THL).
CC {ECO:0000269|PubMed:22194604}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22194604}; Single-pass membrane protein
CC {ECO:0000255}. Note=The catalytic site is on the cytoplasmic side of
CC the inner membrane. {ECO:0000269|PubMed:22194604}.
CC -!- DISRUPTION PHENOTYPE: Inactivation of the mmpL8 gene interrupts the
CC normal biosynthesis of SL-1 and leads to the accumulation of the
CC precursor SL1278. {ECO:0000269|PubMed:22194604}.
CC -!- SIMILARITY: Belongs to the mycobacterial PPE family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46651.1; -; Genomic_DNA.
DR EMBL; CP003248; AFN51848.1; -; Genomic_DNA.
DR EMBL; CP009480; AIR16616.1; -; Genomic_DNA.
DR EMBL; JLDD01000048; KBJ24899.1; -; Genomic_DNA.
DR RefSeq; NP_218339.1; NC_000962.3.
DR RefSeq; WP_003899709.1; NZ_NVQJ01000022.1.
DR AlphaFoldDB; O07801; -.
DR STRING; 83332.Rv3822; -.
DR ESTHER; myctu-Rv3822; PE-PPE.
DR PaxDb; O07801; -.
DR DNASU; 886155; -.
DR GeneID; 886155; -.
DR KEGG; mtu:Rv3822; -.
DR KEGG; mtv:RVBD_3822; -.
DR PATRIC; fig|83332.111.peg.4249; -.
DR TubercuList; Rv3822; -.
DR eggNOG; COG5651; Bacteria.
DR HOGENOM; CLU_061995_1_0_11; -.
DR OMA; SKVPARN; -.
DR PhylomeDB; O07801; -.
DR BioCyc; MetaCyc:G185E-8118-MON; -.
DR BRENDA; 2.3.1.284; 3445.
DR Proteomes; UP000001584; 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:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013228; PE-PPE_C.
DR Pfam; PF08237; PE-PPE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cell inner membrane; Cell membrane; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..404
FT /note="SL1278 acyltransferase Chp1"
FT /id="PRO_0000432823"
FT TOPO_DOM 1..42
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:22194604"
FT DOMAIN 104..325
FT /note="PE-PPE"
FT /evidence="ECO:0000255"
FT MUTAGEN 156
FT /note="S->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:22194604"
SQ SEQUENCE 404 AA; 41408 MW; DEA1FB567438E9AD CRC64;
MKCPGVSDCV ATVRHDNVFA IAAGLRWSAA VPPLHKGDAV TKLLVGAIAG GMLACAAILG
DGIASADTAL IVPGTAPSPY GPLRSLYHFN PAMQPQIGAN YYNPTATRHV VSYPGSFWPV
TGLNSPTVGS SVSAGTNNLD AAIRSTDGPI FVAGLSQGTL VLDREQARLA NDPTAPPPGQ
LTFIKAGDPN NLLWRAFRPG THVPIIDYTV PAPAESQYDT INIVGQYDIF SDPPNRPGNL
LADLNAIAAG GYYGHSATAF SDPARVAPRD ITTTTNSLGA TTTTYFIRTD QLPLVRALVD
MAGLPPQAAG TVDAALRPII DRAYQPGPAP AVNPRDLVQG IRGIPAIAPA IAIPIGSTTG
ASAATSTAAA TAAATNALRG ANVGPGANKA LSMVRGLLPK GKKH
