ID Q087D8_SHEFN Unreviewed; 860 AA.
AC Q087D8;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Peptidase S45, penicillin amidase {ECO:0000313|EMBL:ABI70627.1};
DE Flags: Precursor;
GN OrderedLocusNames=Sfri_0771 {ECO:0000313|EMBL:ABI70627.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI70627.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI70627.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI70627.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; CP000447; ABI70627.1; -; Genomic_DNA.
DR RefSeq; WP_011636250.1; NC_008345.1.
DR AlphaFoldDB; Q087D8; -.
DR STRING; 318167.Sfri_0771; -.
DR MEROPS; S45.004; -.
DR KEGG; sfr:Sfri_0771; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_6; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000000684; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
SQ SEQUENCE 860 AA; 92777 MW; 5A4C5810D22BA363 CRC64;
MKLNKILLAI GMASSVAIVG CGDDTQYGKT PQPDPQPEVV TPPLQAFAPN GTLKVQIRRT
QYGVPHITAD NLESLGFGNG YAQAQDNLCV IADGFIKANS ERSMYFGPHA SIDFTTGLPT
SEDNGNLISD FAYKALKIRQ LAENQYPQFS YNSRALMEGF SAGYNQYLAD VEAGTQTGEP
FCAGQPWVKP ISGVDVASYL FSIALLPGAA NFLDLIFYAN PGDAQEYLPR IVGPAPSTAQ
TAFVQDMNNK LIARSATITT PETNPRNLGS NGWGLGKDKT ENGKGMVLGN PHFPHTGNLR
FWQSHLTIPG QMDVMGGSLA GMPGLVNIGF NKDVAWTHTF STAEHFVMYN LELVAGDRLQ
YMYDNSPMPI NKETVSVLVN AGPAGMLVAQ KDIYTTAKGP MVEAPPTLAP FGWDDGQAFF
IQDANMANKD PLDHWLAMNL ASNKDEFQQA FKNYDGVIFN NTMYADKEGN AFYIDDSTVP
GFSDIVVDII KTTPAIQAAR AQAGFTILPG NTSVFSYDSP MPYERAPKLE RTDFVQNSNN
SFWSTNLAAP LENYSPLYGP ERGQLSLRTR MGLTLMEDAA GDDGKFNIEE LEAALLSNRA
YLAELVLPDL ISQCEQQGAT PVMVSATLSK DVSASCAALK AWNGKQDNDS KGGALLREFA
HQFNQNTMLT EAFDYMSAAT TPNKLNTDGS ALVALAHAAL NLEAAGFAVD VALGDVQFVE
KSLPDGTASG VKLPWPGSHN AEGGFNVFST SLSGDDTLIP QHKYSPVMDV VSGNATASGL
TAEGYQVRYG SSWMMTVSFT DDGPKAKGIL TYSESSNVLS PSFSDQSELY SSTKQLRPLL
FTEAEIQASV ESSIELTLQK
//