CHP2_MYCTU
ID CHP2_MYCTU Reviewed; 359 AA.
AC O50440; I6XXB2; L0T7J5;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Diacyltrehalose acyltransferase Chp2 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000305|PubMed:25124040};
GN Name=chp2 {ECO:0000303|PubMed:25124040};
GN OrderedLocusNames=Rv1184c {ECO:0000312|EMBL:CCP43940.1},
GN RVBD_1184c {ECO:0000312|EMBL:AFN49088.1};
GN ORFNames=LH57_06500 {ECO:0000312|EMBL:AIR13931.1},
GN P425_01234 {ECO:0000312|EMBL:KBJ36430.1};
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, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=25124040; DOI=10.1074/jbc.m114.581199;
RA Belardinelli J.M., Larrouy-Maumus G., Jones V., Sorio de Carvalho L.P.,
RA McNeil M.R., Jackson M.;
RT "Biosynthesis and translocation of unsulfated acyltrehaloses in
RT Mycobacterium tuberculosis.";
RL J. Biol. Chem. 289:27952-27965(2014).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF SER-141.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=25331437; DOI=10.1128/jb.02015-14;
RA Touchette M.H., Holsclaw C.M., Previti M.L., Solomon V.C., Leary J.A.,
RA Bertozzi C.R., Seeliger J.C.;
RT "The rv1184c locus encodes Chp2, an acyltransferase in Mycobacterium
RT tuberculosis polyacyltrehalose lipid biosynthesis.";
RL J. Bacteriol. 197:201-210(2015).
CC -!- FUNCTION: Involved in the final steps of polyacyltrehalose (PAT)
CC biosynthesis. Catalyzes the transfer of three mycolipenoyl groups onto
CC diacyltrehalose (DAT) to form PAT. {ECO:0000269|PubMed:25124040,
CC ECO:0000269|PubMed:25331437}.
CC -!- ACTIVITY REGULATION: Activity is probably potentiated by the DAT/PAT
CC transporter MmpL10. Inhibited by the lipase inhibitor
CC tetrahydrolipstatin (THL). {ECO:0000269|PubMed:25124040,
CC ECO:0000269|PubMed:25331437}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:25124040,
CC ECO:0000269|PubMed:25331437}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant accumulates DAT in the cytoplasm and at
CC the cell surface. Does not produce PAT. {ECO:0000269|PubMed:25124040,
CC ECO:0000269|PubMed:25331437}.
CC -!- MISCELLANEOUS: The topology of this protein is unsure. According to
CC PubMed:25124040, the C-terminal catalytic site is on the periplasmic
CC side of the inner membrane. However, PubMed:25331437 authors conclude
CC that Chp2 has the opposite topology, and that the C-terminal catalytic
CC site is on the cytoplasmic side of the membrane.
CC {ECO:0000305|PubMed:25124040, ECO:0000305|PubMed:25331437}.
CC -!- SIMILARITY: Belongs to the mycobacterial PPE family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43940.1; -; Genomic_DNA.
DR EMBL; CP003248; AFN49088.1; -; Genomic_DNA.
DR EMBL; CP009480; AIR13931.1; -; Genomic_DNA.
DR EMBL; JLDD01000012; KBJ36430.1; -; Genomic_DNA.
DR RefSeq; NP_215700.1; NC_000962.3.
DR RefSeq; WP_003406195.1; NZ_NVQJ01000025.1.
DR AlphaFoldDB; O50440; -.
DR IntAct; O50440; 12.
DR MINT; O50440; -.
DR STRING; 83332.Rv1184c; -.
DR ESTHER; myctu-Rv1184c; PE-PPE.
DR PaxDb; O50440; -.
DR PRIDE; O50440; -.
DR DNASU; 886063; -.
DR GeneID; 45425155; -.
DR GeneID; 886063; -.
DR KEGG; mtu:Rv1184c; -.
DR KEGG; mtv:RVBD_1184c; -.
DR PATRIC; fig|83332.111.peg.1324; -.
DR TubercuList; Rv1184c; -.
DR eggNOG; COG5651; Bacteria.
DR HOGENOM; CLU_061995_1_0_11; -.
DR OMA; MVPPQNI; -.
DR PhylomeDB; O50440; -.
DR BioCyc; MetaCyc:G185E-5353-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:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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 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..359
FT /note="Diacyltrehalose acyltransferase Chp2"
FT /id="PRO_0000432824"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 79..316
FT /note="PE-PPE"
FT /evidence="ECO:0000255"
FT MUTAGEN 141
FT /note="S->A: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25331437"
SQ SEQUENCE 359 AA; 37818 MW; 85E0949ACD144560 CRC64;
MKRVIAGAFA VWLVGWAGGF GTAIAASEPA YPWAPGPPPS PSPVGDASTA KVVYALGGAR
MPGIPWYEYT NQAGSQYFPN AKHDLIDYPA GAAFSWWPTM LLPPGSHQDN MTVGVAVKDG
TNSLDNAIHH GTDPAAAVGL SQGSLVLDQE QARLANDPTA PAPDKLQFTT FGDPTGRHAF
GASFLARIFP PGSHIPIPFI EYTMPQQVDS QYDTNHVVTA YDGFSDFPDR PDNLLAVANA
AIGAAIAHTP IGFTGPGDVP PQNIRTTVNS RGATTTTYLV PVNHLPLTLP LRYLGMSDAE
VDQIDSVLQP QIDAAYARND NWFTRPVSVD PVRGLDPLTA PGSIVEGARG LLGSPAFGG
