ID A6H1P5_FLAPJ Unreviewed; 794 AA.
AC A6H1P5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Penicillin G acylase {ECO:0000313|EMBL:CAL44269.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:CAL44269.1};
GN Name=pac {ECO:0000313|EMBL:CAL44269.1};
GN OrderedLocusNames=FP2213 {ECO:0000313|EMBL:CAL44269.1};
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612 {ECO:0000313|EMBL:CAL44269.1, ECO:0000313|Proteomes:UP000006394};
RN [1] {ECO:0000313|EMBL:CAL44269.1, ECO:0000313|Proteomes:UP000006394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86
RC {ECO:0000313|Proteomes:UP000006394};
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR001227-2};
CC Note=Binds 1 Ca(2+) ion per dimer. {ECO:0000256|PIRSR:PIRSR001227-2};
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; AM398681; CAL44269.1; -; Genomic_DNA.
DR RefSeq; WP_011964303.1; NC_009613.3.
DR RefSeq; YP_001297070.1; NC_009613.3.
DR AlphaFoldDB; A6H1P5; -.
DR STRING; 402612.FP2213; -.
DR MEROPS; S45.003; -.
DR EnsemblBacteria; CAL44269; CAL44269; FP2213.
DR GeneID; 66553316; -.
DR KEGG; fps:FP2213; -.
DR PATRIC; fig|402612.5.peg.2260; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_10; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000006394; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd03747; Ntn_PGA_like; 1.
DR Gene3D; 1.10.1400.10; -; 1.
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; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR043147; Penicillin_amidase_A-knob.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218:SF5; PENICILLIN G ACYLASE; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAL44269.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006394};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 320
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 323
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 794 AA; 91135 MW; D2312D1CF117933A CRC64;
MKKFKKILFV FVLFIAFIAV LLYGYLLSTK PNYEGELFIK NISKETTVYF DDYGVPHIYA
ANQKDAMTAL GYVHAQDRLW QMELIRRIAP GKLAEIFGTR ALKNDKFFIG LGINENSEKA
IATLNKNGKP YQMAMAYLDG VNQYLENGKT PIEFKILGIK KEKFTLKDVY NTFGYMAFSF
AMAQKTDPLL TDIKNKYGEE YLKDLGIDYS LNTTRIKISK EKTQQYIEIS KSITTLLENS
PVPPFIGSNS WVLSPKKTKT GKVLFCNDPH IEYSQPGTWY EAHISCPENE MYGYYLAGTP
FPLLGHNRDY AYGITMFEND DADLFEEENN PKNENQYKTV TGFQNYKIRT KTIKVKDSTS
IILNVKETQH GPIINDLIDN FKNQKPVSFS WIYTQQPNKI LDAVYSLSHA KNMTQFQKGV
SYIVAPGLNI MYGDAKNNIA WFTSGKLYKL EKGVNANLIL NGTNGIDDKK KFLEYAKNPS
AINPSWNYVY SSNNMPEAID GYNYPGYYLP EDRARRITNL LDNKSNWSKE EVSKMTNDNT
SPVSIETVKT MLLVINNKNL SSQEKAAINL LKNWKGTNQL IDVAPTIYTK WLYFYLKNTY
QDEMGEISFK QFLKTHIMKQ SIAFQTKNIN SPWWDNIHTK SKKETRSDIL NMSFKQAISS
LNNQLGNDVN SWTWNKVHKV EYKHPLGSVA LFKPFFNVGK FSISGTNEVI NNTMFDYSDE
AQHIVKAGPS TRRIIDFSDI ENSWSILPTG QSGNPMSTHY NDQAEMYLQG KFRKMKLNKE
EIIKTSTKLI FKAK
//