ID F3FK18_PSESX Unreviewed; 475 AA.
AC F3FK18;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Peptidase S45, penicillin amidase {ECO:0000313|EMBL:EGH30554.1};
DE Flags: Fragment;
GN ORFNames=PSYJA_16857 {ECO:0000313|EMBL:EGH30554.1};
OS Pseudomonas syringae pv. japonica str. M301072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH30554.1, ECO:0000313|Proteomes:UP000004471};
RN [1] {ECO:0000313|EMBL:EGH30554.1, ECO:0000313|Proteomes:UP000004471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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:EGH30554.1}.
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DR EMBL; AEAH01000787; EGH30554.1; -; Genomic_DNA.
DR AlphaFoldDB; F3FK18; -.
DR MEROPS; S45.004; -.
DR HOGENOM; CLU_695455_0_0_6; -.
DR Proteomes; UP000004471; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..475
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003298881"
FT NON_TER 475
FT /evidence="ECO:0000313|EMBL:EGH30554.1"
SQ SEQUENCE 475 AA; 52053 MW; 3AFA8E307AB8A700 CRC64;
MSRPLCGFLF AGLSFAVVLP AQALVEPGSQ AARAEIRRTG FGVPHIVAAN ERGLGYGIGY
AYAQDNLCLL ANEVVTVNGQ RSRYFGPDKA TLEQRNNMAS DLVFQWLNTP QALADFWKAQ
PLEIRQLMQG YVAGYNRSLA EQTTQGLPQP CAAEWVRPIS TDDLVRLTRR LLVEVGVGQF
AEALAGATPP APQKPLQVNA QQVQALQLAA ARNQRFALER GSNAVAIGRE LSANGRGMLL
ANPHFPWAGG MRFYQMHLTI PGKLDVMGAA LPGLPLINIG FNQHLAWSHT VDTSKHFTLH
RLQLDPKDST RYLLDGQSVA MGKQQVSVDV KQPDGSLKSV PRIVYSSIFG PVVQWPGKLD
WDNKFAFSLR DANLQNDRVL QQWYAMDKAD SLKAFEDSVH KIQGIPWVNT LAVDAKGQAL
YMNLSVVPNV DAARLARCSD PRIGTELIVL DGSRSECNWK VSAEAAQAGI YPSSR
//
