ID H0E929_9ACTN Unreviewed; 556 AA.
AC H0E929;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:EHN09807.1};
GN ORFNames=PAI11_33440 {ECO:0000313|EMBL:EHN09807.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN09807.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN09807.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN09807.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:EHN09807.1}.
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DR EMBL; AGUD01000251; EHN09807.1; -; Genomic_DNA.
DR AlphaFoldDB; H0E929; -.
DR PATRIC; fig|1097667.3.peg.3314; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..556
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003531322"
FT DOMAIN 97..286
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 399..497
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 496..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 61319 MW; F921CC9820F57F21 CRC64;
MLARRSAPLL AAGLLAVPAT ADAGQRPPAP PAELQIPARY LQQQIGWVAC SSAVPDLRCA
RVAVPRDWAR PDSGEDIQIA ISKLPTTGGD KRGMVTFNPG GPGASGLGMP IGTGLVHPQL
REHYDLVGFD PRGMGSSRPN VACQTEDEYR AFFGLDGRDR SPQNIARTLQ LSDKTAADCR
TRTGALQPYV TTWQTVRDME FVRRLLDEPR MSYIGYSAGT WLGAHYVQTF PQHADRFVLD
SNVDFTEPWS ENGNLQPLGF ERRFQEDFLP WMARYDRLYH YGTSAREART RYEARRRALQ
AQPLQIAGIT IGPADYDNGV VGVMYSKDGF PVLAQALAAI ERPDALTPDD EAAIQAVFGA
FFDATTYAGY FTITCGDTPW SRDPSDLVRL SERLGRRYPL LGYTWAANPC PFWRQPYGTM
QRIDGRGVPA TLMVNSTHDP ATPYEGARAA HRGFRGSRFV TIRDEGDHGI YGGNPCFDQI
ALRFLIEGVL PRRDSSCPGV PLPDPTAAPA PQAKRAPESL AQQAERLHEQ AESPTEREDR
LGREVGRQLD AALASR
//
