ID A0QQ49_MYCS2 Unreviewed; 399 AA.
AC A0QQ49;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=cutinase {ECO:0000256|ARBA:ARBA00013095};
DE EC=3.1.1.74 {ECO:0000256|ARBA:ARBA00013095};
GN OrderedLocusNames=MSMEG_0625 {ECO:0000313|EMBL:ABK73177.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK73177.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK73177.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
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.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74;
CC Evidence={ECO:0000256|ARBA:ARBA00034045};
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645}.
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; CP000480; ABK73177.1; -; Genomic_DNA.
DR RefSeq; WP_011727075.1; NZ_SIJM01000009.1.
DR RefSeq; YP_885037.1; NC_008596.1.
DR AlphaFoldDB; A0QQ49; -.
DR STRING; 246196.MSMEG_0625; -.
DR PaxDb; 246196-MSMEI_0610; -.
DR GeneID; 66738804; -.
DR KEGG; msm:MSMEG_0625; -.
DR PATRIC; fig|246196.19.peg.622; -.
DR eggNOG; COG1073; Bacteria.
DR OrthoDB; 5416778at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProt.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR22946:SF9; POLYKETIDE TRANSFERASE AF380; 1.
DR PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT DOMAIN 239..360
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 44841 MW; 10F9979319D1B78D CRC64;
MEPSSVDPVD PPIPIPDVPG ADATSRGLPR RIDLTLRQKA IVDASAAADI ALRTGVASVV
AASMLPRTAA TILRRRDSRI EHEHMRFYAD LAEAKDPERS FPRPTEPPRV SSRPANPVAE
WVAHGRVENI RFQSSFRAVN PALRERCRGH VRNNIVRAQH WRHNDGPHPT LCVIHGFMGS
PYLANGLFLS LPWFYRAGYD VLLYTLPFHG LRAERFSPFS GYGYFANGLA GFAEAMAQAV
HDFRSVMDHL EFTGVDRIAL TGISLGGFTS ALLASVDHRI QAVIPNVPVV TPDRTVDEWF
PANMLVALER HIAHTDPELT EAAARYASPL HYQPLVAKER RLIITGLGDR LAPPQQAELL
WEHWDRCAFH WFPGNHLLHV SQPDYLRRMT RFLRGFMFD
//
