ID S9SIJ3_9RHOB Unreviewed; 824 AA.
AC S9SIJ3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Protein related to penicillin acylase {ECO:0000313|EMBL:EPX86159.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:EPX86159.1};
GN ORFNames=ruthe_00968 {ECO:0000313|EMBL:EPX86159.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX86159.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX86159.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX86159.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
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:EPX86159.1}.
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DR EMBL; AOLV01000010; EPX86159.1; -; Genomic_DNA.
DR RefSeq; WP_021097067.1; NZ_KE557320.1.
DR AlphaFoldDB; S9SIJ3; -.
DR STRING; 1123069.ruthe_00968; -.
DR MEROPS; S45.003; -.
DR PATRIC; fig|1123069.3.peg.939; -.
DR HOGENOM; CLU_011790_0_1_5; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000015346; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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, ECO:0000313|EMBL:EPX86159.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 263
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 523
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 824 AA; 90316 MW; 77C567785969EB1D CRC64;
MATLFRWLFR ATVTLILLGL LGFGLVWWLA ARSLPDYDGE RTVSGITAPV EIVRDHSNVP
HIFGQTDADV FFGLGYAHAQ DRLWQMIVLR RTAQGRLSEV FGARTLPIDR LLRRLDLYGL
ATASVAAQDE TTLAALEAYS AGVNAWLHEI NAEARGRGAP EMWLFPQAVA PWQPADSLAL
LKLMALQLNG HLEAEVRRAR LSLVLPPERV ADLMPEAPGP GVAALPRYAD LVPAEGLPRF
AAADPAPRDP LMPAAPLPLA GASNAWAAGV SRTASGSTLL ASDPHLPLSA PGLFYLARIE
LTSGGVIGGT IPGIPAILSG RSADLGWGIT SSWLDDLDVY AEEVNPRNAG EYRTPDGWAP
FRTRDSIIQV KDAPAETLHL QWTANGPVLG PEDFNLGLVR PPGHVMAVSW TALSDRDTTM
TAAIRLMRAQ NIEEALEAAR LFVAPSQNLV VADRNRIAMT TMGTLPVRDP AHQSQGRMPT
LGWIAQNRWL GVKAPEANPV WIDPEGGIVG NTNNKVIDAP FPDHLSWLWG DSQRVQRWRF
LMQAREIHTR ESFIEAQLDT VSPAARTLLP LVGRDLWFTG EAAPDGTPER LRQRALALLA
EWNGQMNEHL PEPLIYAAWM RALQERLIRD DLGPLADEFT QVEPLFIERV FRNVDGASAW
CDVRQSAPVE TCTDIARLAL DDALLWIRER WGTQIESLRW GDAHEAVHAH PVLGSIPLLS
WFVNIRQSTS GDDQTLMRGV TAGTEAEPFR NVHAAAYRGV YDFADPDSSV FIIATGQSGH
PLSPHYDDLG VLWRRGEYIP MSLDPALARA AAVGITRLLP ESAE
//
