CUP6H_MYCS2
ID CUP6H_MYCS2 Reviewed; 337 AA.
AC A0R619; I7GAQ7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Carboxylesterase Culp6 homolog {ECO:0000305};
DE EC=3.1.1.- {ECO:0000269|PubMed:20656688};
GN OrderedLocusNames=MSMEG_6394 {ECO:0000312|EMBL:ABK70327.1},
GN MSMEI_6226 {ECO:0000312|EMBL:AFP42652.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4] {ECO:0007744|PDB:3AJA}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 36-337, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, DISULFIDE BONDS, AND ACTIVE SITE.
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=5.22 mM for pNP-butyrate {ECO:0000269|PubMed:20656688};
CC Vmax=783 nmol/min/mg enzyme with pNP-butyrate as substrate
CC {ECO:0000269|PubMed:20656688};
CC Note=kcat is 0.448 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 -!- DISRUPTION PHENOTYPE: Essential, cannot be disrupted.
CC {ECO:0000269|PubMed:20656688}.
CC -!- SIMILARITY: Belongs to the cutinase family. {ECO:0000305}.
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DR EMBL; CP000480; ABK70327.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42652.1; -; Genomic_DNA.
DR RefSeq; WP_011731258.1; NZ_SIJM01000013.1.
DR RefSeq; YP_890607.1; NC_008596.1.
DR PDB; 3AJA; X-ray; 2.90 A; A/B=36-337.
DR PDBsum; 3AJA; -.
DR AlphaFoldDB; A0R619; -.
DR SMR; A0R619; -.
DR STRING; 246196.MSMEI_6226; -.
DR ESTHER; mycs2-a0r619; Cutinase.
DR PRIDE; A0R619; -.
DR EnsemblBacteria; ABK70327; ABK70327; MSMEG_6394.
DR EnsemblBacteria; AFP42652; AFP42652; MSMEI_6226.
DR GeneID; 66737672; -.
DR KEGG; msg:MSMEI_6226; -.
DR KEGG; msm:MSMEG_6394; -.
DR PATRIC; fig|246196.19.peg.6221; -.
DR eggNOG; COG4223; Bacteria.
DR OMA; TLNWAQG; -.
DR OrthoDB; 1884001at2; -.
DR EvolutionaryTrace; A0R619; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 3D-structure; Cell membrane; Disulfide bond; Hydrolase; Membrane;
KW Reference proteome; Serine esterase; Transmembrane; Transmembrane helix.
FT CHAIN 1..337
FT /note="Carboxylesterase Culp6 homolog"
FT /id="PRO_0000450111"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 41..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..59
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000305|PubMed:20656688"
FT ACT_SITE 269
FT /evidence="ECO:0000305|PubMed:20656688"
FT ACT_SITE 300
FT /evidence="ECO:0000305|PubMed:20656688"
FT DISULFID 73..165
FT /evidence="ECO:0000269|PubMed:20656688,
FT ECO:0007744|PDB:3AJA"
FT DISULFID 265..272
FT /evidence="ECO:0000269|PubMed:20656688,
FT ECO:0007744|PDB:3AJA"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:3AJA"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3AJA"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 143..164
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 177..190
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:3AJA"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3AJA"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3AJA"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:3AJA"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:3AJA"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:3AJA"
FT HELIX 316..330
FT /evidence="ECO:0007829|PDB:3AJA"
SQ SEQUENCE 337 AA; 35888 MW; 0F9ABB54321E9EBE CRC64;
MAKNARRKRH RILALIAAAA MALVVVLVVT IVVVIMRRPD TPATPPPSAE PPGGVVVPPG
TRKPRPEFQS ADCPDVMMVS IPGTWESSPT DDPFNPTQFP LSLMSNISKP LAEQFGPDRL
QVYTTPYTAQ FHNPFAADKQ MSYNDSRAEG MRTTVKAMTD MNDRCPLTSY VIAGFSQGAV
IAGDIASDIG NGRGPVDEDL VLGVTLIADG RRQMGVGQDV GPNPAGQGAE ITLHEVPALS
ALGLTMTGPR PGGFGALDNR TNQICGSGDL ICSAPEQAFS VFNLPKTLET LSGSAAGPVH
ALYNTPQFWV ENGQTATQWT LEWARNLVEN APHPKHG
