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Database: UniProt
Entry: A0A235I9C1_9NOSO
LinkDB: A0A235I9C1_9NOSO
Original site: A0A235I9C1_9NOSO 
ID   A0A235I9C1_9NOSO        Unreviewed;       846 AA.
AC   A0A235I9C1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:OYD94064.1};
GN   ORFNames=CDG76_17130 {ECO:0000313|EMBL:OYD94064.1};
OS   Nostoc sp. 'Peltigera membranacea cyanobiont' 210A.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=2014529 {ECO:0000313|EMBL:OYD94064.1, ECO:0000313|Proteomes:UP000215440};
RN   [1] {ECO:0000313|EMBL:OYD94064.1, ECO:0000313|Proteomes:UP000215440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=210A {ECO:0000313|EMBL:OYD94064.1,
RC   ECO:0000313|Proteomes:UP000215440};
RA   Gagunashvili A.N., Andresson O.S.;
RT   "Distinctive characters of Nostoc genomes in cyanolichens.";
RL   Submitted (JUL-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}.
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:OYD94064.1}.
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DR   EMBL; NOLJ01000005; OYD94064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A235I9C1; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000215440; 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:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 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   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        285
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         363
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         366
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   846 AA;  95782 MW;  0877E1ED896D2918 CRC64;
     MKNSRKGWLR KRLKITLIFL LVLGLLLVGF STYTVRQSFP QESGTIQLPE LKAEVIVQRD
     KWGVPHIYAA NSHDLFMAQG YIHAQDRFWQ MDFWRHIGSG RLSEMFGSSQ VDTDKYLRTM
     GWARVAQQEI QEINAEMKAY LEAYADGVNA YLAEHQGSAL SLEYAVLKFL NPGYKPEPWQ
     ILHSLTWGKV MAYDLGRNFE SEIERAILLK TLTHTQVEEL FPPYPQDLPV ILPELQQGEG
     AGKGRNKNVE VLLNSPDILP ALESITKPMI ALEKLIGPTG IGIGSNNWVI SGQRTTTGKP
     ILANDPHLGV QIPSIWYEVG LHCTPKSAEC PYNVSGFSFA GMIGVIIGHS DRIAWGVTNV
     QSDVMDLYIE KINPKNPNQY EVNGKWVDMQ LVPETIQVAG SQTIVQTVRY TRHGPILSDV
     SPNLKDFKPS KSLELPQNYA VALRWTALAP SKLGYAIPQI NRAQNWQEFR SAASNYDVPA
     QNLVYADIDG NIGYQMPGKF PIRAQGDGRY PIPGWTDEYE WQGYIDFEKL PKNFNPSQGY
     IATANNLVMR EYPYLITADW VYGYRAKRIV EMILQQTQPI SLKDVQQIQG DNRNLNAQTL
     VPLLQSIAVD TPRLQAAQKL LQGWNLQLEM TSPAAALFEV FWKHLLADTF HDQLPEKYFP
     DGGDRWYAVI ANLVKQPNSA WWDNRNTPKI ENRDQILRQS FIKAVDELEG IQSKNPNNWN
     WGKLHTITFR NATLGKSGVA PIEALFNRGA FATSGNGETV NANRWRANKS FEVTDIPSLR
     MIVDLGNLDN SVAIHTPGQS GHAFHSHYND MVEPWRKTEY HQMLWELKNV TENTTATLRL
     IPKLVE
//
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