ID J1RMH4_9ACTN Unreviewed; 907 AA.
AC J1RMH4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:EJJ05619.1, ECO:0000313|EMBL:QTZ92421.1};
GN ORFNames=SU9_013785 {ECO:0000313|EMBL:QTZ92421.1}, SU9_17712
GN {ECO:0000313|EMBL:EJJ05619.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ05619.1};
RN [1] {ECO:0000313|EMBL:EJJ05619.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ05619.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ92421.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ92421.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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; AJGV01000104; EJJ05619.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ92421.1; -; Genomic_DNA.
DR RefSeq; WP_006605073.1; NZ_CP072931.1.
DR AlphaFoldDB; J1RMH4; -.
DR STRING; 1160718.SU9_17712; -.
DR MEROPS; S45.003; -.
DR KEGG; sauh:SU9_013785; -.
DR PATRIC; fig|1160718.3.peg.3580; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_11; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000009036; Chromosome.
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; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009036};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 301
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 211
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 379
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 382
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 907 AA; 99930 MW; 5BD3FF97E84B11D2 CRC64;
MPANKSGPVP RKKKGRRGRL VAITVVLLLV AGIGFGAFWG VSTVRASFPQ TTGSLKVPGL
TNPVDVTRDA NGIPQIYADT DEDLFRAQGY VQAQDRFWEM DVRRHMTAGR LSEMFGKSQV
KTDSFLRTMG WHRVAQKEYD TKLSPATKKY LQSYSAGVNA YLKDHEGSAL SLEYAALDFQ
NDYKPEKWTP VDSVAWLKAM AWDLRGNMQE EIDRSLMTSR FTPAQINQLY PAYPYKRNKP
IVEGGSVDSA TKQFKPGAAA NSAPAGAAGA AAGYQSQLSS LSKTLDKVPA LLGPNGNGIG
SNSWVVSGAH TTTGKPLLAN DPHLAPQMPS LWYQMGLHCR TTSPKCNYDV SGFTFSGMPG
VVIGHNQDVS WGMTNLGADV TDLYLEKVNA DGYLYDNRQR PFVTRKETIK VAGGESREIT
VRSTGNGPIV SDRDGELAGV GKDAPVGNAA PDRGDGYAVS LRWTALNPGK SMDAVFELNR
AKNWTDFRKA AGHFEVPSQN LIYADTKGNI GYQAPGQIPV RGKGDGGFDG TYPAPGWDPK
YRWTGYLPQK SLPYEYNPKR GYIVTANQAV TDEKYPYLLT KDWGYGSRSQ RINDLIQSKI
KDGGKVSTDD MQAFQKDNSS EIARLLTPYL TKIDIKDKYV RDAQQLLEGW DFTQEPDSAA
AAYFNAVWRN TLKLAFGNKM PKELRPDGQC LTVRPADETG PADENDKYVR ECGERAGDTA
QPDGGDRWYE VVRGILDDPN NAWWKTEDRP GRPGDKNRDQ LLAHAMADAR YELTSKLGKN
IDNWSWGRLH QMFLKNQTLG TDGPGMLQGL FNRGPWNVGG GEAAVDATGW NAAGGYNVTW
VPSMRMVVNL ADLDKSRWIN LTGASGHAYD AHYYDQTDKW AKGELLPWAY SEDAVKKAGK
DTLTLSP
//
