ID   A0A1M3EFE3_9CELL        Unreviewed;       855 AA.
AC   A0A1M3EFE3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:OJV56991.1};
GN   ORFNames=BGO38_03430 {ECO:0000313|EMBL:OJV56991.1};
OS   Cellulomonas sp. 73-145.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV56991.1, ECO:0000313|Proteomes:UP000184491};
RN   [1] {ECO:0000313|EMBL:OJV56991.1, ECO:0000313|Proteomes:UP000184491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-145 {ECO:0000313|EMBL:OJV56991.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJV56991.1}.
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DR   EMBL; MKTI01000013; OJV56991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3EFE3; -.
DR   STRING; 1895739.BGO38_03430; -.
DR   Proteomes; UP000184491; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        284
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         362
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         365
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   855 AA;  90754 MW;  129932325C5789EB CRC64;
     MARPRVVRTA LVTVAAIVVL VLVAVVVGGV VVLRRPLPTS SGTLSLPGLT RPVTVMRDAR
     GVPTITATSA TDLFRAQGFV AAQDRFFQMD YRRHVTAGRL SELVGADARA LEADKVVRTL
     GWHRVAEQEW GLLDATTQSY LTAYAEGVNS YLATRDPGSI AVEYTVLGLR VQVAQPEPWQ
     PVDSLAWLKA MAWDLRSNYE DELGRARAYR TIGDVGKVDE LFPTYPQQLN APILPSGGDA
     TVVPTVARAQ LPLGDGQAQD AFAAADRALT AVPVLLGTGA ATGSNSWAVS GAHTASGKPI
     LANDPHLELT APGIWSQVGL RCQQVSADCP FDVSGFGFAG MPGVVIGHDA KLAWGLTNMG
     ADVTDLFLER VDDRSGTQLV NGAQVPLQVR HETIRVNGGN DVDLVVRTTT HGPIISDVLD
     LSGATSAPTP DRSTSAFQVS LGWTASTPGR TAEAIFRLDA AATAADVAAA AALFDVPAQN
     IVFATTDGHI GYQAPGRIPI RETVPGDVPS DGSWPRPGWD SAYDWQGWVP SAQLPHVLDP
     PEGFVVAANQ AVLPQGTGPF LTADYDMGYR SQRIRTLLTQ QIAAGKKIDV ASTQAVQDDT
     HSPMADVLLP ALLKVDLGSG FEADGQRLLR TWDGSMSADS AAAAYFAAVW NNVLRLTFAD
     DLPDHDAPTN DSRWIEVMRH IVDAPDSPWW DDRSTLGVVE GRDGVLRNAM IAARQQLTAQ
     LGVRADEWRW GLLHQVRLEH PLLGGAGQPG VLRGAVNPAA QQVGGGSSSV DATGWDPSTG
     GYSVTAGPSM RMVVDLADLD SSTWVDLTGT SGHPASPHYS DQLSTWAAGR QFPWPFSAAA
     TQADARSRLT LQPSA
//