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Database: UniProt
Entry: A0A177QKS5_9PLAN
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ID   A0A177QKS5_9PLAN        Unreviewed;       792 AA.
AC   A0A177QKS5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptidase S45 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYO44_07240 {ECO:0000313|EMBL:OAI48361.1};
OS   Planctomycetaceae bacterium SCGC AG-212-F19.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae.
OX   NCBI_TaxID=1799658 {ECO:0000313|EMBL:OAI48361.1, ECO:0000313|Proteomes:UP000186541};
RN   [1] {ECO:0000313|Proteomes:UP000186541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC AG-212-F19 {ECO:0000313|Proteomes:UP000186541};
RA   Choi J., Stepanauskas R., Howe A.;
RL   Submitted (FEB-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:OAI48361.1}.
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DR   EMBL; LSTD01000245; OAI48361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A177QKS5; -.
DR   Proteomes; UP000186541; 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   Reference proteome {ECO:0000313|Proteomes:UP000186541};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..792
FT                   /note="Peptidase S45"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008071555"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         194
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         331
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         334
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   792 AA;  87873 MW;  04D886C092E7FF15 CRC64;
     MRMLRAVAVL LLSAALVMSA PAQQAETPEA VLQKAKAVLA QLDGAIKLPG IKEPVEVLRD
     RWGVPHIYAK NTDDLFFAQG FVVAQDRLFQ IDLWRRIAIG ETSEVLGKKG LEADRFARLV
     KYRGDMQAEW TSYAPDTQQI ATAFTRGINA AIDHKGERLP IEFQILGYKP AKWQPEDILG
     RMSGIIMTRN FRDEVLRAEL VAAVGVEKAR RIAPTNPVRE YGPAAGLDLA GIDRSILAGY
     DAATRVLPFA LRGKGDEGSN NWAIDGNLSA SGKPMMASDP HRPINLPSLR YLAHLNAPGW
     NVIGAGEPAL PGIALGHNER VAWGFTIVGT DQADLFVEET KPGEPTQYKI GEKWEAMKVV
     KEKVTIKGAP AVELELRFTR HGPVIHEDAK RNRAFALRWA GSEPGGAAYL PSLALDRVQS
     ARDFVAALSR WKLPSLNMVH ADVDGNIGWV AAAATPIRDR WDGLLPAPGK DHDWQGFREL
     RHLPQEHNPA RGYIVTANHN ILPLAYPHEI AYEWAVPFRY LRLKERLDAK KQFTIDDSKH
     MQHDNVSIAG RRLARLAQSM TARDPALEPY IFALREWHGD LSVDSRPGVL YGFWLQEMLD
     AFFRPHVPPN LLEFARGRHG IEVMLTALEK PDEFWFGKDP PAGAQLFLRS TLAAAIPRIK
     KALGPNEKEW TWGKLHTTTL RHPLAQLGPV YEKAFNLGPV PKAGDGFTPH AAAHNAKFEQ
     LTGASYRHIF DLADWDKGVA TSVPGQSGQP GSAHYGDLLP LWAEGQYFPL AYSRKKVEEV
     TVHRLMLQPA AK
//
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