ID A0A1S6FJG6_9SPHN Unreviewed; 785 AA.
AC A0A1S6FJG6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:AQR73789.1};
GN ORFNames=BXU08_09140 {ECO:0000313|EMBL:AQR73789.1};
OS Sphingomonas sp. LM7.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1938607 {ECO:0000313|EMBL:AQR73789.1, ECO:0000313|Proteomes:UP000189383};
RN [1] {ECO:0000313|EMBL:AQR73789.1, ECO:0000313|Proteomes:UP000189383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM7 {ECO:0000313|EMBL:AQR73789.1,
RC ECO:0000313|Proteomes:UP000189383};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019511; AQR73789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6FJG6; -.
DR STRING; 1938607.BXU08_09140; -.
DR KEGG; splm:BXU08_09140; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000189383; 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 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:UP000189383};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..785
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010545840"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 507
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 785 AA; 85007 MW; 811E8E76AE0B212E CRC64;
MFDRRFFLLG SVATLALAPA AVARVQLARP VRDAAVRGLD APIEIVDDAY GVPHIRAASI
PDAFFGQGYV VARDRMFQVD LSHRRELGRL AEVFGADFAK HDATARLFHY RGDLDAELRS
VPENVLACAR AYVAGINARI DEVLADPALL PLEYGILGIA PLRWELRDLV LARGASIDNA
DDEVRRAQLA ALGLLDLDAI IAPLRPSWKM TVPEGLNPAA VSEADLGMLQ LGSLPFSAET
PVADPAAGPE TRANAGSNAW TVAPSRSATG RPILANDPHL GIGGFGPRHV AHLSAPGLDV
IGGGSPGLPG IMQGHTDRFA FGRTNFHIDQ LDLFVLELDP SDPERYRHDG GWKAFRKVEV
AIPVKGGAPY VTVLRYCAQG PVVSHDPARR RATAVASIGM QPGGHGAFAM IAINLAKDWK
SLKKAFPLHP SPTNFHYADV DGNTGWQVIG FAPVRRKGEG LLPVPGDGRY DWTGMRNFTA
LPSEYNPSKG WFASANQNNL PADWPRDRIP AFSFRDPYRY ERIVDVLSQQ DKHRLIDSVA
LHHDTFSEPA RQLVALLPVR PSPASDMLRG WDARIDGASG AAALFEILWR DLGKRMLAAI
VPVRAKHLVR EVAPSVLLGL LAKPDARLGA DPMAARDAML DAALVAAWAS AHELMGSDPA
TWRWDALHQV RIQHPLSRIP AIAKAFPPIE GEGSGGDSYT VMARWLGSGP GWRTGGGASY
LQVIDVGAWD NSLMLNLPGQ SNDPRSPHHR DQYAPWIAGA MQPMLFSKAA VDARATGRTQ
LRPKR
//