ID Q6KYV6_PICTO Unreviewed; 815 AA.
AC Q6KYV6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:AAT44096.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:AAT44096.1};
GN OrderedLocusNames=PTO1511 {ECO:0000313|EMBL:AAT44096.1};
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828 / KAW 2/3).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=1122961 {ECO:0000313|EMBL:AAT44096.1, ECO:0000313|Proteomes:UP000000438};
RN [1] {ECO:0000313|EMBL:AAT44096.1, ECO:0000313|Proteomes:UP000000438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828
RC {ECO:0000313|Proteomes:UP000000438};
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Futterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; AE017261; AAT44096.1; -; Genomic_DNA.
DR RefSeq; WP_011178312.1; NC_005877.1.
DR AlphaFoldDB; Q6KYV6; -.
DR STRING; 263820.PTO1511; -.
DR MEROPS; S45.003; -.
DR PaxDb; 263820-PTO1511; -.
DR GeneID; 2844651; -.
DR KEGG; pto:PTO1511; -.
DR eggNOG; arCOG04082; Archaea.
DR HOGENOM; CLU_011790_4_0_2; -.
DR InParanoid; Q6KYV6; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAT44096.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 815 AA; 93120 MW; F51E95DF9C3B231B CRC64;
MLKKRFFTGL IVIIIVFILL FISLTPLSPF YELLNPETGI YARPPPYSSG VSTFTIERDN
RSASVTVYYE NCLGFIGIYS NHNWSLFYEQ GYLEARYRLA QIEIIKAEAT GTLASIIGKS
ELSSDILSRE LLNCPVAREE FQNLSRSSYT YMALSNFVAG INSYINGLTY KDMPLLFKTL
NYRPGDWNVT DVLAIQQSFL WENTPANFDP LYFQYALEKM PENIVRALYP AYPAGIQNPI
VPYKCNPSVY KETGDINNLS LYTPSVNITG NLNFSVSRCL EFPSSRSFSN DWAVNGIKTD
NTSALLANDP HLTTSVPSIW MGFQLVSPGM NVIGVVFPGF PGIILGHNRY IAWGATNGQI
QETYFYAEVS KGYTYLSYNK WLHYKIINET IDVRGSSPYH LMIRIANNGV VMFNESGTEI
AMDWTGMHPT YEITFFLNID RSRDIKGFVS NLTKYFKVAV QNWAVADSNG NIGIYPYGEY
PVIEHGDPRG ILNGTGISNW IGFVPLRYEP YLYDPARGFV FSDNQITVSD NYPYYIGWDY
ESGYRADEAY HLLNSSYDVN TDKMKSIQLT VHDYTTNIFL KPLLRAISRY YYNTSYYNEL
SNWNGNMSIN STAATIFYFW ENNTLNDTFM PYMEKYNINQ SNGLFNVSFF LGPDDMYHGP
LIEDLVNWTL NDPYSRYFDN PLNGETRNFY TIALTAFNQT IMYLNERYGG IPAWGNIHKR
YLVSFFGINA MNTMDVPAAG DGNTINAAYG IISDFGPSWR LIVNMSRPED AIGIYPGGIS
ENPLSKYYDN NFIPWNNGLY YKIMPENEPE VFRYE
//
