ID A4XBB0_SALTO Unreviewed; 779 AA.
AC A4XBB0;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Peptidase S45, penicillin amidase {ECO:0000313|EMBL:ABP56209.1};
GN OrderedLocusNames=Strop_3778 {ECO:0000313|EMBL:ABP56209.1};
OS Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS 105044 / CNB-440).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP56209.1, ECO:0000313|Proteomes:UP000000235};
RN [1] {ECO:0000313|Proteomes:UP000000235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC {ECO:0000313|Proteomes:UP000000235};
RX PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA Jensen P.R., Moore B.S.;
RT "Genome sequencing reveals complex secondary metabolome in the marine
RT actinomycete Salinispora tropica.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; CP000667; ABP56209.1; -; Genomic_DNA.
DR RefSeq; WP_012014984.1; NC_009380.1.
DR AlphaFoldDB; A4XBB0; -.
DR STRING; 369723.Strop_3778; -.
DR MEROPS; S45.005; -.
DR KEGG; stp:Strop_3778; -.
DR PATRIC; fig|369723.5.peg.3898; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_11; -.
DR Proteomes; UP000000235; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
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; 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 SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000235};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
SQ SEQUENCE 779 AA; 83115 MW; D717E6FFE9C823C1 CRC64;
MSPRRLAAAA TVVGLVTAGL TVTGGAATAN GGGYSALIQR ASYGVPHITA RDFASLGFGA
GYVQAEDNIC LIADQMVTVR AERSRWFGAE AGNVSSDLFH QKAIDDQVAE QLLAGSRDGV
RAPSTPVRDQ VRGFVAGYNA YLRDGKAITD PACAGKEWVD PISELDMWRA YWARMVLASS
GALIDGIVAA APPTASGNGE SAHAPQAEAA VATVDGAPAG LGSNAYGLGR DGTTSGASIL
LANPHFPWDD TERFYRMHLK VPGRYDVEGA ALVGDPLIQI GHNGQIAWSH TVSTAHRFVW
HRLALVPGDP TSYLYDGQAR KMTARTVTVQ TPTGPISRTL YDTHFGPVVV VPGHFDWTTT
TAYAITDANA TNNRALDGWL AMGRAGSVGE LRKVLDRRQF LPWVNVIAVD RRGRALYADH
SVVPRVTDSL AAACIPAPFQ SVYASSGQAV LDGSRSSCEL GRDPDAAVPG ILGPANLPTL
VRSDYVTNSN DSYWLANPEH PLEGYPRIVG DEQTQRSLRT RLGVHQVRQR LTGIDGLPGK
GFTTSNLWDV TLGNRAYGGE LVRDDLVRSC EARPTATTSD GATVDLTAAC AALRGWDLRV
DLDSRGAHLF TEFAMAGGLR FADPFDPTAP LTTPSRLAVD DPGVRTALAD AVQKLAGIRL
DARLGDIQTE PRGAEQIPIH GGRSEAGAFN MINGGFESGV GYPKVLHGTS FLMAVELGSN
GPSGRQILTY SQSANPNSPW YADQTRLYSG KGWDTIKFTQ RQLRADPNLV TYRVGEQRD
//
