CULP2_MYCTU
ID CULP2_MYCTU Reviewed; 230 AA.
AC P9WP41; L0TAS9; P63881; Q50664;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Probable carboxylesterase Culp2 {ECO:0000305};
DE EC=3.1.1.- {ECO:0000250|UniProtKB:P9WP43};
DE AltName: Full=CFP25 {ECO:0000303|PubMed:9673225};
DE AltName: Full=Cutinase-like protein 2 {ECO:0000303|PubMed:19225166};
DE Short=Culp2 {ECO:0000303|PubMed:19225166};
DE Flags: Precursor;
GN Name=cut2; OrderedLocusNames=Rv2301; ORFNames=MTCY339.08c;
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 PROTEIN SEQUENCE OF 44-58, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=9673225; DOI=10.1128/iai.66.8.3492-3500.1998;
RA Weldingh K., Rosenkrands I., Jacobsen S., Rasmussen P.B., Elhay M.J.,
RA Andersen P.;
RT "Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis
RT culture filtrate and purification and characterization of six novel
RT proteins.";
RL Infect. Immun. 66:3492-3500(1998).
RN [3]
RP FUNCTION.
RX PubMed=10076913; DOI=10.1111/j.1574-695x.1999.tb01235.x;
RA Weldingh K., Andersen P.;
RT "Immunological evaluation of novel Mycobacterium tuberculosis culture
RT filtrate proteins.";
RL FEMS Immunol. Med. Microbiol. 23:159-164(1999).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=H37Rv;
RX PubMed=19225166; DOI=10.1096/fj.08-114421;
RA West N.P., Chow F.M., Randall E.J., Wu J., Chen J., Ribeiro J.M.,
RA Britton W.J.;
RT "Cutinase-like proteins of Mycobacterium tuberculosis: characterization of
RT their variable enzymatic functions and active site identification.";
RL FASEB J. 23:1694-1704(2009).
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 SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RX PubMed=21594640; DOI=10.1007/s00726-011-0938-7;
RA Ocampo M., Rodriguez D.M., Curtidor H., Vanegas M., Patarroyo M.A.,
RA Patarroyo M.E.;
RT "Peptides derived from Mycobacterium tuberculosis Rv2301 protein are
RT involved in invasion to human epithelial cells and macrophages.";
RL Amino Acids 42:2067-2077(2012).
CC -!- FUNCTION: Shows weak esterase activity with the p-nitrophenol-linked
CC aliphatic ester pNP-butyrate. Does not exhibit cutinase activity.
CC {ECO:0000269|PubMed:19225166}.
CC -!- FUNCTION: Induces interferon-gamma (IFN-gamma) release in animal models
CC and in human TB patients (PubMed:9673225, PubMed:10076913). Also
CC induces a strong delayed-type hypersensitivity (DTH) response in animal
CC models (PubMed:9673225). {ECO:0000269|PubMed:10076913,
CC ECO:0000269|PubMed:9673225}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19225166,
CC ECO:0000269|PubMed:9673225}. Cell surface
CC {ECO:0000269|PubMed:21594640}.
CC -!- BIOTECHNOLOGY: Five Rv2301 high activity binding peptides (HABPs) could
CC be included as components of an antituberculosis vaccine.
CC {ECO:0000269|PubMed:21594640}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP45083.1; -; Genomic_DNA.
DR RefSeq; NP_216817.2; NC_000962.3.
DR RefSeq; WP_003411863.1; NZ_NVQJ01000012.1.
DR AlphaFoldDB; P9WP41; -.
DR SMR; P9WP41; -.
DR STRING; 83332.Rv2301; -.
DR ESTHER; myctu-cutas2; Cutinase.
DR PaxDb; P9WP41; -.
DR DNASU; 885371; -.
DR GeneID; 885371; -.
DR KEGG; mtu:Rv2301; -.
DR TubercuList; Rv2301; -.
DR eggNOG; ENOG5033WEM; Bacteria.
DR OMA; DDPICNP; -.
DR PhylomeDB; P9WP41; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042783; P:evasion of host immune response; IMP:MTBBASE.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000675; Cutinase/axe.
DR InterPro; IPR043580; CUTINASE_1.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR33630; PTHR33630; 1.
DR Pfam; PF01083; Cutinase; 1.
DR SMART; SM01110; Cutinase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00155; CUTINASE_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Reference proteome;
KW Secreted; Serine esterase; Signal; Virulence.
FT SIGNAL 1..43
FT /evidence="ECO:0000269|PubMed:9673225"
FT CHAIN 44..230
FT /note="Probable carboxylesterase Culp2"
FT /id="PRO_0000006449"
FT ACT_SITE 123
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 189
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT ACT_SITE 207
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT DISULFID 45..112
FT /evidence="ECO:0000250|UniProtKB:O53581"
FT DISULFID 185..192
FT /evidence="ECO:0000250|UniProtKB:O53581"
SQ SEQUENCE 230 AA; 23926 MW; 3707CA5016AEE5A3 CRC64;
MNDLLTRRLL TMGAAAAMLA AVLLLTPITV PAGYPGAVAP ATAACPDAEV VFARGRFEPP
GIGTVGNAFV SALRSKVNKN VGVYAVKYPA DNQIDVGAND MSAHIQSMAN SCPNTRLVPG
GYSLGAAVTD VVLAVPTQMW GFTNPLPPGS DEHIAAVALF GNGSQWVGPI TNFSPAYNDR
TIELCHGDDP VCHPADPNTW EANWPQHLAG AYVSSGMVNQ AADFVAGKLQ
