ID A0A1T5PCP5_9BACT Unreviewed; 808 AA.
AC A0A1T5PCP5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SKD10357.1};
GN ORFNames=SAMN05660461_6266 {ECO:0000313|EMBL:SKD10357.1};
OS Chitinophaga ginsengisegetis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=393003 {ECO:0000313|EMBL:SKD10357.1, ECO:0000313|Proteomes:UP000190166};
RN [1] {ECO:0000313|EMBL:SKD10357.1, ECO:0000313|Proteomes:UP000190166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18108 {ECO:0000313|EMBL:SKD10357.1,
RC ECO:0000313|Proteomes:UP000190166};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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; FUZZ01000006; SKD10357.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5PCP5; -.
DR STRING; 393003.SAMN05660461_6266; -.
DR Proteomes; UP000190166; Unassembled WGS sequence.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF2; J DOMAIN-CONTAINING PROTEIN; 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};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000190166};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 209
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 808 AA; 90608 MW; CF258E3BC2BF976A CRC64;
MRIIPAVITA AITLSLTYAF SHKLGQIPPL GKLLSPQTGF WQNAEPIGEF PREQLVLPGL
SGKTEVWYDD RMVPHIFAEN EGDAYYVQGY VTARDRLWQM ELQTYAAAGR LSEILGPKLV
QYDRKQRRLG MVYAAEGTVK EMLADPATKV AVTSYAAGVN AYIATLTPAT YPVEYKILDY
KPERWDIIKS ALLLKYMAHD LAGFANDLEF TNARRLFSLQ DFDLMYPDFH EATDPIIPKG
TPYPAATIKP TAPPDSVLAA AAAYMKFKTD KPDPDNGSNN WAVGGSKTRS GAPILCSDPH
LSLSLPSLWY EVQIHTPDMN VYGASLPGAP GVIIGFNDHI AWGVTNGEED VKDYYSMQFR
NGRSEYLYNG SYRKADLRIE EIKVRGGATV RDTVAYTVFG PVMFDNTFPD KTAGQTFLAM
RWKALDPSNE LATFNKLNKA RNYDDYLNAL NRYTCPAQNF VFADKAGDIA IWHNGQYPLR
WKDQGKWIMP GSDSTYAWQG FIPHEELPHI KNPERGFVSS ANQRPTDSTY PYALYGEYDL
FRGKRINERL SAMSAITTQD MMQLQNDDKN LFAAAAMPMI RKHIDTSSLT AQQQPYWQLL
TSWDFMATPD SKAASIFNAL WAHLEDTIWH DELHPKDTTI LTYPQSITTL QLLLRDTAFH
FIDNINTPQK ETLSQLLQGA FAQTVTELSE LNKAGRLELG KARGTDINHL SRGIPAFSAL
HLNTGGGQHI VNATKQTHGP SWRMVVQLSD KTEAYGIYPG GQSGNPGSPF YDNSVNDWVS
GKYYMLHIFS AEEKDDPVIR YKLVFTGK
//