ID I0KXX0_9ACTN Unreviewed; 537 AA.
AC I0KXX0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=cutinase {ECO:0000256|ARBA:ARBA00013095};
DE EC=3.1.1.74 {ECO:0000256|ARBA:ARBA00013095};
GN ORFNames=MILUP08_41331 {ECO:0000313|EMBL:CCH16417.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH16417.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCH16417.1}.
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DR EMBL; CAIE01000013; CCH16417.1; -; Genomic_DNA.
DR RefSeq; WP_007456254.1; NZ_HF570108.1.
DR AlphaFoldDB; I0KXX0; -.
DR STRING; 1150864.MILUP08_41331; -.
DR eggNOG; COG1073; Bacteria.
DR OrthoDB; 504769at2; -.
DR Proteomes; UP000003448; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008806; F:carboxymethylenebutenolidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR PANTHER; PTHR22946:SF9; POLYKETIDE TRANSFERASE AF380; 1.
DR PANTHER; PTHR22946; UNCHARACTERIZED; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CCH16417.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..457
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 464..483
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..171
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
FT REGION 287..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 53711 MW; A9BB2F9B338D2114 CRC64;
MSAASPHHPP STRAAVLLAV LAALAAALGT AVLVRADAGL SVRQVTVGGV PMTEVRAGPP
TADARRPGVV IAHGFAGSAR LMRPIADTVA RRGAVALLFD FAGHGASRAR LGPDMSPATL
AADLDAAVGH LRAQPDVDPA QIMLVGHSMG AGAVTRYAAG HPEIARTVAI SLPDAGELPP
GRPAELLLIV GGAEFPAFRR AADDAVGRGA SVGRRPAVVV PGVEHISVLF APRTHEEIAD
WLPSVDGTAA PRPLVRLAGA ALLLLAFAVG VVPLAALLLG RRGTGSPGPG GGPALAGSPG
PAGSPALTGG PTPAGARVPL GGAALLGLAV LATGVGAAVA ALLPTNRLPL AVGGYVTGFL
LVSGLLVIAG QRLLPGRSRT PGTWQTPGTI VDPADGRAPA GAVGAALALT AYAVVAVALP
IHLGLTSALP VGARWWLLPL VVAACLLFLL GVELVAAGRT WRRLLVVAVT VLVLSTSAVV
GVAPGFVLLV VPLFAVLLGW HVLWAAVLRR YAAPRWLPAL VGAALLGWPI ATTLPLR
//
