LIPC_MYCTU
ID LIPC_MYCTU Reviewed; 403 AA.
AC P96402; F2GM18; I6WXR6; Q7DA89;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Esterase LipC {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:22038913};
GN Name=lipC {ECO:0000303|PubMed:22038913};
GN OrderedLocusNames=Rv0220 {ECO:0000312|EMBL:CCP42948.1};
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] {ECO:0007744|PubMed:21969609}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=H37Rv;
RX PubMed=22038913; DOI=10.1128/iai.05541-11;
RA Shen G., Singh K., Chandra D., Serveau-Avesque C., Maurin D., Canaan S.,
RA Singla R., Behera D., Laal S.;
RT "LipC (Rv0220) is an immunogenic cell surface esterase of Mycobacterium
RT tuberculosis.";
RL Infect. Immun. 80:243-253(2012).
CC -!- FUNCTION: Esterase that can hydrolyze short-chain esters with the
CC carbon chain containing 2 to 10 carbon atoms. Does not have lipase
CC activity. Is highly immunogenic and elicits strong humoral immune
CC responses in both HIV-negative (HIV-) and HIV-positive (HIV+)
CC tuberculosis (TB) patients. Also elicits pro-inflammatory cytokine and
CC chemokine responses from macrophages and pulmonary epithelial cells
CC (PubMed:22038913). May participate in the progression of active
CC tuberculosis both by contributing to the utilization of lipid
CC substrates for bacterial growth and replication, and by modulating
CC immune responses (PubMed:22038913). {ECO:0000269|PubMed:22038913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol
CC + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748;
CC Evidence={ECO:0000269|PubMed:22038913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:22038913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) +
CC hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656;
CC Evidence={ECO:0000269|PubMed:22038913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622;
CC Evidence={ECO:0000269|PubMed:22038913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657;
CC Evidence={ECO:0000269|PubMed:22038913};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate +
CC H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658;
CC Evidence={ECO:0000269|PubMed:22038913};
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:22038913}.
CC Secreted, cell wall {ECO:0000269|PubMed:22038913}. Secreted, capsule
CC {ECO:0000269|PubMed:22038913}. Note=Cell surface protein that is
CC present in both the cell wall and the capsule.
CC {ECO:0000269|PubMed:22038913}.
CC -!- DEVELOPMENTAL STAGE: Expressed only during active M.tuberculosis
CC infection. {ECO:0000269|PubMed:22038913}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP42948.1; -; Genomic_DNA.
DR RefSeq; NP_214734.1; NC_000962.3.
DR RefSeq; WP_003899863.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; P96402; -.
DR SMR; P96402; -.
DR STRING; 83332.Rv0220; -.
DR ESTHER; myctu-Rv0220; Hormone-sensitive_lipase_like.
DR PaxDb; P96402; -.
DR PRIDE; P96402; -.
DR DNASU; 886722; -.
DR GeneID; 45424191; -.
DR GeneID; 886722; -.
DR KEGG; mtu:Rv0220; -.
DR PATRIC; fig|83332.111.peg.251; -.
DR TubercuList; Rv0220; -.
DR eggNOG; COG0657; Bacteria.
DR OMA; EQGWVCL; -.
DR PhylomeDB; P96402; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0042603; C:capsule; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008126; F:acetylesterase activity; IEA:RHEA.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:MTBBASE.
DR GO; GO:0046503; P:glycerolipid catabolic process; IDA:MTBBASE.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR Pfam; PF07859; Abhydrolase_3; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
PE 1: Evidence at protein level;
KW Cell wall; Hydrolase; Reference proteome; Secreted.
FT CHAIN 1..403
FT /note="Esterase LipC"
FT /id="PRO_0000448850"
FT ACT_SITE 237
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 334
FT /evidence="ECO:0000250|UniProtKB:O06350"
FT ACT_SITE 367
FT /evidence="ECO:0000250|UniProtKB:O06350"
SQ SEQUENCE 403 AA; 44308 MW; 4FBAB5F1DECDC563 CRC64;
MNQRRAAGST GVAYIRWLLR ARPADYMLAL SVAGGSLPVV GKHLKPLGGV TAIGVWGARH
ASDFLSATAK DLLTPGINEV RRRDRASTQE VSVAALRGIV SPDDLAVEWP APERTPPVCG
ALRHRRYVHR RRVLYGDDPA QLLDVWRRKD MPTKPAPVLI FVPGGAWVHG SRAIQGYAVL
SRLAAQGWVC LSIDYRVAPH HRWPRHILDV KTAIAWARAN VDKFGGDRNF IAVAGCSAGG
HLSALAGLTA NDPQYQAELP EGSDTSVDAV VGIYGRYDWE DRSTPERARF VDFLERVVVQ
RTIDRHPEVF RDASPIQRVT RNAPPFLVIH GSRDCVIPVE QARSFVERLR AVSRSQVGYL
ELPGAGHGFD LLDGARTGPT AHAIALFLNQ VHRSRAQFAK EVI
