ID A0A0B4XJ13_9GAMM Unreviewed; 848 AA.
AC A0A0B4XJ13;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative penicillin amidase {ECO:0000313|EMBL:AJD47031.1};
GN ORFNames=S7S_03045 {ECO:0000313|EMBL:AJD47031.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD47031.1, ECO:0000313|Proteomes:UP000006764};
RN [1] {ECO:0000313|EMBL:AJD47031.1, ECO:0000313|Proteomes:UP000006764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W11-5 {ECO:0000313|EMBL:AJD47031.1,
RC ECO:0000313|Proteomes:UP000006764};
RX PubMed=23209202; DOI=10.1128/JB.01845-12;
RA Lai Q., Shao Z.;
RT "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT type strain W11-5, isolated from deep sea sediment.";
RL J. Bacteriol. 194:6936-6936(2012).
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 -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC from the same precursor. {ECO:0000256|ARBA:ARBA00038735}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; CP004387; AJD47031.1; -; Genomic_DNA.
DR RefSeq; WP_008740051.1; NZ_CP004387.1.
DR AlphaFoldDB; A0A0B4XJ13; -.
DR STRING; 391936.S7S_03045; -.
DR MEROPS; S45.003; -.
DR KEGG; apac:S7S_03045; -.
DR HOGENOM; CLU_011790_0_1_6; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000006764; 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 GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000006764};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT ACT_SITE 259
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 848 AA; 92853 MW; 78D924322BD2990E CRC64;
MRHWIRALLL GGLALATTGC MEGWLDKWLA ASVDPQTGTL HVEGLAAPVT IGRDALGIPL
VEAESFEDLA FATGWVMAED RLSQMVGFTM AAQGRLAEMA GEVALPMDLY SRTLGLRRIS
EQQLAAGSDE LTFLLQRFSD GVNAWLVAHE DRMPLDFRLG SFRPEPWAPI NSVDVFTMIN
LGLGVNLHEE IMALNLADRV GTDRLPWLVP VYPDEPLSFA EAAKLNDLPL PALAKQAQAL
DAARDGFERL LMPQGLAASN NWVVAPSHST TGHSLLANDT HLLISQPPMW MLLHQKTPGI
QVAGVAAAGM PVPVIGFNGN VAWGATMVMA DAQDLFLEQL RDIDGQLHYL ADGEWLPVTE
REEVFKVQGG DTVTHTVRST RHGPLLESVL NAPPISPVVP PRLADSMARY GLAFSWTASQ
ADTTMDAMFA LGRSQSLAEA REHIRGVRFI HLNMVMADQD AAGWQVTGRY PQRKQGTGQF
PSPGWDGVYD WTGFADFDQH PNDFTLEKGF VGTANHRTVA ADYPLLLSRS WFYPQRGDRI
NQLLSAKAKH SAEDMVAMQA DRFDRFVPAL QAVLSDNSVA LATAINALPS ARQAPARQAL
AMLDNFDGVM LEDSAAAALY GVFFHLAARN IFLDELGPED GPVWQSFTRM TLLSYSAPQD
HLLQREDSPF WDNAGTPETE TKWDIFAQTL ADAWAFNTQA LGDDPAQWAW GDLHTYEWKT
AASQMKPWLP RVQRWAISAM EGYLNRGPYP AGGNHNTLNV AGAMIGRDFD VHSIPAMRMV
VDFAADEPLQ LVNSGGQSGN PASPHYDDGI DVWLGWGNRT LPFSEAGRAA HYAQRLTLTP
SEAPAATP
//
