GenomeNet

Database: UniProt
Entry: A0A0B4XU92_9GAMM
LinkDB: A0A0B4XU92_9GAMM
Original site: A0A0B4XU92_9GAMM 
ID   A0A0B4XU92_9GAMM        Unreviewed;      1030 AA.
AC   A0A0B4XU92;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Peptidase S45 penicillin amidase {ECO:0000313|EMBL:AJD49842.1};
GN   ORFNames=S7S_17150 {ECO:0000313|EMBL:AJD49842.1};
OS   Isoalcanivorax pacificus W11-5.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Isoalcanivorax.
OX   NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD49842.1, ECO:0000313|Proteomes:UP000006764};
RN   [1] {ECO:0000313|EMBL:AJD49842.1, ECO:0000313|Proteomes:UP000006764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W11-5 {ECO:0000313|EMBL:AJD49842.1,
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   -!- 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP004387; AJD49842.1; -; Genomic_DNA.
DR   RefSeq; WP_041026029.1; NZ_CP004387.1.
DR   AlphaFoldDB; A0A0B4XU92; -.
DR   STRING; 391936.S7S_17150; -.
DR   MEROPS; S45.001; -.
DR   KEGG; apac:S7S_17150; -.
DR   HOGENOM; CLU_311672_0_0_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:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
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:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 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:UP000006764};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1030
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002112168"
FT   REGION          20..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1030 AA;  111354 MW;  4B1BBE2C8ED4A0A2 CRC64;
     MNRLTLLAAL ASLLLTACGG SGSSTRNTAP GNEPEPPRNE ERTPIPVTQP FADHGTVLNI
     LPPGQDDNGG VSNLLQEIPG LGDLLGSLLD DGVSQTGLVP ALIREPHFDD QLGLYEDLAF
     SPPGLTDDQL TDYFKAAPLL PPDAGGWTAE SQITSGDYRV DIRRDTFGVP HIFGASRLDA
     LFGMGYVTAQ DRLFLLDVLR RAGRGELSKF LGPADFSFDL DIAGQAPYRE ADRTAQIAQV
     ASALGEDGAQ IFKDATAFVD GLNKYVLDAR SGLLQVPIEY VGLGVTLEPF VIEDVVAIAT
     LIQGIFAGGG GAEHQNVLLL HELAARYGDP EEACALWRDL RHANDPESSV TTATRFATQS
     PARINEDACP LLPEFASEYP GAVMFDAGSF VAHNPLVTEP CGRPGQVQCP GVAGGLPALP
     LTGVVEVIIN GTMELLRGLL SLSDASDVVI PLRPDGQLSS TDQMLAARTP LRMPLDTRIA
     ALDDSALWQA QRSAQAALAG IAQLRDGFPA TMSNALLVNG EHTASGHPIA VFGPQTSYFV
     PQLLLEMAVH GGDLHTRGMT FTGLPYVVIG RGPDFAWSAT SGNSDLTDVK VLPLCAPGGG
     GARDGYIYRG RCVAFDVIDD SWSARWNVAV PAGDPLATGQ NVKVTRHIIR SPHIGPVLGY
     ATVNGQAVAL VRQRSTYFAE LDTALPFLLA TRNDVFDAQS FREVFNLTTG SFNWFYIDDQ
     DISFIHAGLY PRRAEGVHPE LPSWGDGRYD WQGFLSLEEH PQDTNPARGF LASWNNRPAP
     DWWSADDNAS YQLVHRNDML EMRLEKLVAD GNVTRGSLTE AMGDAAVTDL RGQEILPAAL
     ALLQRGTLTS AQQEAVFMLH DWVDVGAPRR DRDNDGRYDQ EDAVALMDAW YPRMIEQLLP
     QILPLEATDF GNLMPVGRDN KPGDMGSAYQ HGYYGYLRRV LDMANGDSGA PYRALRCAGS
     DNATFCRAQL LGSLDQALTD LGGIGNRDNW LVDMTQDSIE HRAIGLAGLR PIHWQNRPTF
     QQVVEFTSSR
//
DBGET integrated database retrieval system