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Database: UniProt
Entry: A0A1B7Z6K8_9FLAO
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Original site: A0A1B7Z6K8_9FLAO 
ID   A0A1B7Z6K8_9FLAO        Unreviewed;       798 AA.
AC   A0A1B7Z6K8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:OBR38349.1};
GN   ORFNames=A9200_17790 {ECO:0000313|EMBL:OBR38349.1};
OS   Maribacter hydrothermalis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1836467 {ECO:0000313|EMBL:OBR38349.1, ECO:0000313|Proteomes:UP000092164};
RN   [1] {ECO:0000313|Proteomes:UP000092164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T28 {ECO:0000313|Proteomes:UP000092164};
RA   Zhan P.;
RL   Submitted (JUN-2016) 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}.
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:OBR38349.1}.
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DR   EMBL; LZFP01000014; OBR38349.1; -; Genomic_DNA.
DR   RefSeq; WP_068485080.1; NZ_LZFP01000014.1.
DR   AlphaFoldDB; A0A1B7Z6K8; -.
DR   STRING; 1836467.BTR34_15620; -.
DR   KEGG; mart:BTR34_15620; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000092164; 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: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};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092164};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        250
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         322
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         324
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   798 AA;  89945 MW;  3CB8AA0577A4FF04 CRC64;
     MRTLKKLGFI LLLLITILVI ATGVIVYTLK PDYSGEQELV HLQKEVKVYY DTYGIPHIYG
     ENEQDAFRTL GYVHAQDRLW QMELLRRIAS GGLSEVFGKD LVGTDKFFLS LGIADASKKT
     VANSNRNDEG VVLAEAYLDG INQFIKEGPT PVEFYLTGID KKEFVLEDVY NTIGYMAFSF
     AMAHKTDPLL TTINAKLGPE YLKDLSISSD TTTVWIENYN PSQKDSLQNN LTAVVNKALG
     VLNVPLFEGS NSWVIAPEKT KNGKVILAND PHIGFAQPSV WYEAHIETPT YSKYGYHIAG
     IPFPLLGHNR ASAYGITMFE NDDVDFYYEQ NNPENDGQYL TSNGYVDYEI VEKTIKVKDT
     SSVEFTYKKS VHGPILNGIA DQIQDERPIA MSWIYTQMDN KVIDALFGLS HSNTLSEFRA
     ALPNIHAPGL NIMYGDAEGN VGWFASAQLY SIPDSINTKM IYEVGKGLPI EKELLAFNQN
     PQAINPPSNY VYSANNQPDS IAGMLYPGYY LPENRAKRIV ELLEPKNDWD KESVSDMITD
     VTSAIDPVIV SNLSKYIDIN LLSENGLRVI DSLKMWNGDY KLVSSEATVF NRWIYHLLKN
     TFKDELGEDL FNQLLTTHFV KRLIAPLSKN ENSVWWDNVN TNEETERMAA IVNKSFTDAI
     ASLEKDFGAN GENWQWEKVH TIEHEHPIGQ IETLRSFFNV GPYPIEGGRE VINNLAFSYD
     DTGYYKTSSG PSTRRVIDFS DVENSISILP TGQSGNPFSS HYKDQAEMYV NGEFRKMMMN
     ETEIKNTSNS ILIFSPNQ
//
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