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Database: UniProt
Entry: A0A0H3C741_CAUVN
LinkDB: A0A0H3C741_CAUVN
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ID   A0A0H3C741_CAUVN        Unreviewed;       700 AA.
AC   A0A0H3C741;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Penicillin acylase {ECO:0000313|EMBL:ACL94542.1};
DE            EC=3.5.1.11 {ECO:0000313|EMBL:ACL94542.1};
GN   OrderedLocusNames=CCNA_01077 {ECO:0000313|EMBL:ACL94542.1};
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050 {ECO:0000313|EMBL:ACL94542.1, ECO:0000313|Proteomes:UP000001364};
RN   [1] {ECO:0000313|EMBL:ACL94542.1, ECO:0000313|Proteomes:UP000001364}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N {ECO:0000313|Proteomes:UP000001364};
RX   PubMed=20472802; DOI=10.1128/JB.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
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}.
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DR   EMBL; CP001340; ACL94542.1; -; Genomic_DNA.
DR   RefSeq; WP_012640121.1; NC_011916.1.
DR   RefSeq; YP_002516450.1; NC_011916.1.
DR   AlphaFoldDB; A0A0H3C741; -.
DR   GeneID; 7329828; -.
DR   KEGG; ccs:CCNA_01077; -.
DR   PATRIC; fig|565050.3.peg.1060; -.
DR   HOGENOM; CLU_021155_0_0_5; -.
DR   OrthoDB; 9760084at2; -.
DR   PhylomeDB; A0A0H3C741; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   CDD; cd01936; Ntn_CA; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR   PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   PIRSF; PIRSF001227; Pen_acylase; 2.
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, ECO:0000313|EMBL:ACL94542.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001364};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   REGION          186..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
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         271
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         273
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         274
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   700 AA;  76569 MW;  7F2C606BC85B3F5B CRC64;
     MKWILRGIGG LLALVLIAAL ALIAIDRASL PQAPSRQALL DKAKAYDVRI RRDEWGVPHI
     LGRTDADAAF GLGYAQSEDD FDTLQDVVLA TRGVLARDKG AGAAPTDYVV SLLEVWPTVD
     KHYAELPAEL RAIMEAYADG VSLYVAKHPE KAKPGLLPVT GKDVAAGFIF KQPFFYGLDG
     ELRRITAPAT KGPPPKGSNG LATAPSRSVD GATRLLVNSH QPYTGPVAWY EAVVQSGQGW
     HVAGGFFPGS PFMLHGHNAT LGWANTVSKP DLVDVYRLTI NPANKNQYRL DGQWKDFDKR
     YVTLRVKLLG PIVLPVRKAV LRSAHGPVLE TDHGVFAIRY AGMGEWRQPL QYWRLNRART
     VEDWRAAIAT HAIPSLNYVY ADAAGNIGFV HNGQYPNRRA KADWGGVLPG DRSDLIWQGY
     LPVENSPQLW NPKSGLVFNS NNTPFEASEA ADNLKPADFP ASMGLQANMT NRAWRALETY
     GADRALTDAS FRAHKFDVAF SDRSSVMAMV GEVLAVDPKG DADLAEAQRI LRAWDKRADR
     TNRGAALAAL MSQPILFANT NGDPAPAPID SLRAAIKTLK THFGRLDPEW GEVNRIRRGT
     VDLPIDGAAD TFRSVWGKPQ KDGTTTADGG DTFVMFVTWD KAGALRSESI HQFGSATLDA
     ASPHYADQTP LFVAMKTKPV RFTEDQLQGH IKVDYRPGER
//
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