ID D9PZG9_ACIS3 Unreviewed; 646 AA.
AC D9PZG9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Acylamino-acid-releasing enzyme {ECO:0000313|EMBL:ADL18457.1};
DE EC=3.4.19.1 {ECO:0000313|EMBL:ADL18457.1};
GN OrderedLocusNames=ASAC_0049 {ECO:0000313|EMBL:ADL18457.1};
OS Acidilobus saccharovorans (strain DSM 16705 / JCM 18335 / VKM B-2471 /
OS 345-15).
OC Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC Acidilobus.
OX NCBI_TaxID=666510 {ECO:0000313|EMBL:ADL18457.1, ECO:0000313|Proteomes:UP000000346};
RN [1] {ECO:0000313|EMBL:ADL18457.1, ECO:0000313|Proteomes:UP000000346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16705 / JCM 18335 / VKM B-2471 / 345-15
RC {ECO:0000313|Proteomes:UP000000346};
RX PubMed=20581186; DOI=10.1128/AEM.00599-10;
RA Mardanov A.V., Svetlitchnyi V.A., Beletsky A.V., Prokofeva M.I.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "The genome sequence of the crenarchaeon Acidilobus saccharovorans supports
RT a new order, Acidilobales, and suggests an important ecological role in
RT terrestrial acidic hot springs.";
RL Appl. Environ. Microbiol. 76:5652-5657(2010).
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DR EMBL; CP001742; ADL18457.1; -; Genomic_DNA.
DR RefSeq; WP_013265969.1; NC_014374.1.
DR AlphaFoldDB; D9PZG9; -.
DR STRING; 666510.ASAC_0049; -.
DR GeneID; 9498260; -.
DR KEGG; asc:ASAC_0049; -.
DR eggNOG; arCOG01646; Archaea.
DR eggNOG; arCOG03383; Archaea.
DR HOGENOM; CLU_008615_2_1_2; -.
DR InParanoid; D9PZG9; -.
DR Proteomes; UP000000346; Chromosome.
DR GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADL18457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000346}.
FT DOMAIN 433..644
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 646 AA; 72053 MW; 463B0F59CC728547 CRC64;
MSPEDLSKLT LVSSPAASPD GSRALFVVSR PDLQQNRYDS SIWLYDGRSY YPVTSGPGDS
CPAWSPDGQT IAFIRTVRQE GQPAQTSVML MRPGYEPVPL FTWSFGASAI SWSPAGSSIA
FLARRPLGQG EWKDYSKREA LVIERLPPFF NGEGYIFDRP RNIYLVSANG GEPRRLTSHA
LDVSDFAWSP DGRSIAYVKQ LEEVHAQYDE LRLINVETGE DVQLLSKVSI AGLAWSSDGN
SIALLMHRFE RGLSSHYKLH SYNLKTGELT KVELGLDRNL LNSVNSEARG PSCTKPIQAS
GGWLYFSVSD AGRAWLYRAT LSGRVEPVLR PEDAVIDDFS VAQSSDVVYY TQMNESEPAE
LYVLRGTSGK RLTSFNDDFL RQASLPRAFK ARARARDGTE LDFWALLPRD AKGKVPWMLY
IHGGPKTSYG YGFMVAFHVL ASAGIAVVYG NPRGSDGYSE DFADIRGRWG TVDYEDLMTI
ADEATRQFQQ LDPGRAGVAG GSYGGFMTNW VITHTSRFRA AMTERSCVEF YSDWGTSDIG
WFFDEDQLMA QPPWKSAEQY LKASPMTYIE SVTTPLLIMH ALEDYRCPVS QALQLFTALK
VLGVEVKLAL FPGEDHDLTR SGRPKTRVEY LKLMLDWMKG HLGEGR
//
