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Database: UniProt
Entry: A0A1F8Q1F6_9CHLR
LinkDB: A0A1F8Q1F6_9CHLR
Original site: A0A1F8Q1F6_9CHLR 
ID   A0A1F8Q1F6_9CHLR        Unreviewed;       789 AA.
AC   A0A1F8Q1F6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 22.
DE   RecName: Full=Peptidase S45 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A2W33_02685 {ECO:0000313|EMBL:OGO29290.1};
OS   Chloroflexi bacterium RBG_16_52_11.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797646 {ECO:0000313|EMBL:OGO29290.1, ECO:0000313|Proteomes:UP000179327};
RN   [1] {ECO:0000313|EMBL:OGO29290.1, ECO:0000313|Proteomes:UP000179327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO29290.1}.
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DR   EMBL; MGNN01000010; OGO29290.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8Q1F6; -.
DR   Proteomes; UP000179327; 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        240
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         312
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         315
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   789 AA;  89474 MW;  FDE96AFEA7974505 CRC64;
     MPKQDTIIGS IARNGLTWLS RRRLPLIEGS LKFAGIKSTA EVIRDRWGIP HIYAQDMQDL
     FFAQGFVHAQ DRLFQMELNR RVAQGRLSEI FGEIALDTDR TARTFGFNRL GRTDWSNISG
     DLREIILAYT AGVNAYLDHS ERKLPVEFTL LRFEPEAWTP EDTASFTRVM IWQLSHAWYG
     EVLRAQLIEA VGESHAGELE IQYPENNPIT LPKGIEYNRL DNENLRQKVG GPFLHQGKGS
     NAWAVSGDRS ATGKPILCND MHLQLSTPSL WYQNHLIAGD FNVTGVSLAG LPLVLVGHNS
     HVAWGMTLAF TDCEDLFVEK FNPQQPNHYQ FKDTWEESEQ IPEPINVKGL AEPHMEMVTV
     TRHGPVISDV IGYPEQRVSV NSMALRPCMA FEGWYSLNKA HMWGDFVDAM RLIEAPQLNV
     CYADIDGNVG YWVTGRVPIR AKGDGSLPAP GWTGEYEWIE EVPFEEMPHA LNPEQGYIVT
     CNHKLVDADY PYLLGNVWMN GYRARRIVDY FESKGKLTFD DHRAMHIDFT CLPGKEMIAL
     LDELTSTDPD VQLAQNILNA WDCNLTPNSV GGTLYEVTRY YLVRNVLESG LGEEMAFRVM
     GRGFHPLLMP THEFYGHDTV AVLRILNNQD SWWLEQVKGR EAVLAQSLKQ AVEWLRAYLG
     EDHTEWQWGK IHRALFPHAM GIQKPLDQVF NLGPYPIGGD TDTPCQTAFY AHDPYDLKAW
     APSFRQIVDL GDLSRSVMIV PPGQSGQLGS PHYDDLIQPW LNGEYAPQLW TREQVESHAL
     GKLILSRLS
//
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