ID   CUP6H_CORGL             Reviewed;         309 AA.
AC   Q8NLR5; Q6M1Y5;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Carboxylesterase Culp6 homolog {ECO:0000305};
DE            EC=3.1.1.- {ECO:0000269|PubMed:20656688};
GN   OrderedLocusNames=Cgl2873 {ECO:0000312|EMBL:BAC00267.1};
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=20656688; DOI=10.1074/jbc.m110.150094;
RA   Crellin P.K., Vivian J.P., Scoble J., Chow F.M., West N.P., Brammananth R.,
RA   Proellocks N.I., Shahine A., Le Nours J., Wilce M.C., Britton W.J.,
RA   Coppel R.L., Rossjohn J., Beddoe T.;
RT   "Tetrahydrolipstatin inhibition, functional analyses, and three-dimensional
RT   structure of a lipase essential for mycobacterial viability.";
RL   J. Biol. Chem. 285:30050-30060(2010).
CC   -!- FUNCTION: Esterase that may be involved in cell wall biosynthesis
CC       and/or maintenance. Hydrolyzes pNP-butyrate (C4).
CC       {ECO:0000269|PubMed:20656688}.
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:20656688};
CC   -!- ACTIVITY REGULATION: Inhibited by tetrahydrolipstatin (THL), a specific
CC       lipase inhibitor. {ECO:0000269|PubMed:20656688}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.71 mM for pNP-butyrate {ECO:0000269|PubMed:20656688};
CC         Vmax=273 nmol/min/mg enzyme with pNP-butyrate as substrate
CC         {ECO:0000269|PubMed:20656688};
CC         Note=kcat is 0.146 sec(-1) with pNP-butyrate as substrate.
CC         {ECO:0000269|PubMed:20656688};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR   EMBL; BA000036; BAC00267.1; -; Genomic_DNA.
DR   RefSeq; NP_602065.1; NC_003450.3.
DR   RefSeq; WP_011015453.1; NC_006958.1.
DR   AlphaFoldDB; Q8NLR5; -.
DR   SMR; Q8NLR5; -.
DR   STRING; 196627.cg3180; -.
DR   ESTHER; corgl-q8nlr5; Cutinase.
DR   KEGG; cgl:Cgl2873; -.
DR   PATRIC; fig|196627.13.peg.2805; -.
DR   eggNOG; COG4223; Bacteria.
DR   HOGENOM; CLU_882318_0_0_11; -.
DR   OMA; TLNWAQG; -.
DR   Proteomes; UP000000582; 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:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000675; Cutinase/axe.
DR   PANTHER; PTHR33630; PTHR33630; 1.
DR   Pfam; PF01083; Cutinase; 1.
DR   SMART; SM01110; Cutinase; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Hydrolase; Membrane; Reference proteome;
KW   Serine esterase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..309
FT                   /note="Carboxylesterase Culp6 homolog"
FT                   /id="PRO_0000450110"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        157
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        253
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        55..146
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
FT   DISULFID        249..256
FT                   /evidence="ECO:0000250|UniProtKB:O53581"
SQ   SEQUENCE   309 AA;  32616 MW;  0FD7E6F7F45CF48B CRC64;
     MRKTITVIAV LIVLALIGVG IVQYVNTSDD SDFIGQPGEP TGTETTEPPV QPDWCPAVEV
     IAAPGTWESA ANDDPINPTA NPLSFMLSIT QPLQERYSAD DVKVWTLPYT AQFRNINSQN
     EMSYDDSRNE GTAKMNEELI NTHNECPATE FIIVGFSQGA VIAGDVAAQI GSEQGVIPAD
     SVRGVALIAD GRREPGVGQF PGTFVDGIGA EVTLQPLNLL VQPIVPGATM RGGRAGGFGV
     LNDRVQDICA PNDAICDAPV NVGNALDRAL AMVSANGVHA LYATNPDVFP GTTTNAWVVD
     WATNLIDNG