ID A0A1P9WY19_9BACT Unreviewed; 688 AA.
AC A0A1P9WY19;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Peptidase S45 {ECO:0000313|EMBL:AQG80250.1};
GN ORFNames=AWR27_13540 {ECO:0000313|EMBL:AQG80250.1};
OS Spirosoma montaniterrae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1178516 {ECO:0000313|EMBL:AQG80250.1, ECO:0000313|Proteomes:UP000187941};
RN [1] {ECO:0000313|EMBL:AQG80250.1, ECO:0000313|Proteomes:UP000187941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY10 {ECO:0000313|EMBL:AQG80250.1,
RC ECO:0000313|Proteomes:UP000187941};
RA Oliw E.H.;
RL Submitted (JAN-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}.
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DR EMBL; CP014263; AQG80250.1; -; Genomic_DNA.
DR RefSeq; WP_077131675.1; NZ_CP014263.1.
DR AlphaFoldDB; A0A1P9WY19; -.
DR STRING; 1178516.AWR27_13540; -.
DR KEGG; smon:AWR27_13540; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000187941; Chromosome.
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 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; 3.
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:UP000187941};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..688
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012817612"
FT ACT_SITE 181
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 688 AA; 77883 MW; AB11F8EC727DC371 CRC64;
MKPYRLLAFL LLLTQSLHAQ INPASVTIAR DTFGVPHIFA KADAEVAYGL AWAHAEDNFR
TIQLLVMPAK GLLGRQLGKT GAAADYVVEL LHAPELVAAE GDKALSPDFR AVLEGYLQGL
NDYARTHPAD VINKRLFPLT VADYLKTSVL SLSVISGVER ALKAIYDGKV SGIDGLKPAG
SNAIAVHRNK TVEDETMLAI NSHQPLEGPV AWYEAHLCSE QGWNALGGLF PGGATIFHGV
NEHLAWAHTV NYQDKIDTYQ LQTDNAHPNE YLFDNQWLTL DQKRVRLRVK GIPFAIGRKA
YWSKYGPTIK TKRGWFALRT GSFMELRGME QWYRMNKARS FSEFRQALQM TAIPGFNIIY
ADRDTIFYVS NGKIPYRDPA YDWSGTLPGN TAKTLWTKFR PLSDFPQYVN PPSGYLFNMN
HTPFNATGSA DNLRPEQFDK TMGYERWNTN RSLRFMELIG QYDKLSYADF KRIKYDLQLP
KTLSYAQGPD ANALFTLRPD THPDIREQIE MLTNWNRQAT TDSRGATTFL VFYHYWQDKL
QHEGRQSNAT RMLTADECAE GLRHVKTYLQ KYFGRTDVAL GDYQKHVRGP KELPVWGIPD
VLASIYAKPY RNGLVRSDAG ESYIELVRFP KTGLPIIESI NCFGASAHPD SPHYTDQMEL
FVQMKTKPMT LDKAAVLQTA KRIYHPGE
//
