ID A1ARP5_PELPD Unreviewed; 452 AA.
AC A1ARP5;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:ABL00016.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:ABL00016.1};
GN OrderedLocusNames=Ppro_2409 {ECO:0000313|EMBL:ABL00016.1};
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966 {ECO:0000313|EMBL:ABL00016.1, ECO:0000313|Proteomes:UP000006732};
RN [1] {ECO:0000313|EMBL:ABL00016.1, ECO:0000313|Proteomes:UP000006732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1
RC {ECO:0000313|Proteomes:UP000006732};
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP000482; ABL00016.1; -; Genomic_DNA.
DR RefSeq; WP_011736271.1; NC_008609.1.
DR AlphaFoldDB; A1ARP5; -.
DR STRING; 338966.Ppro_2409; -.
DR MEROPS; S41.004; -.
DR KEGG; ppd:Ppro_2409; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_1_1_7; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000006732; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ABL00016.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ABL00016.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006732};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 93..161
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 380..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 50033 MW; BD041FAE7AC14276 CRC64;
MVSMGSKKRR VFAGLVIAMA TLVIFIGISS QPRSRAEAQG SDYESIELFT DVMAIIKKSY
VEEVDTKKLI YGAINGMLAS LDPHSSFMSP ETYKEMKIDT KGAFGGLGIE ITVKDGVLIV
IAPIEDTPAF KAGIKAGDHI FKIDGKFTKD MNINDAVKRM RGPKGTKVVL SIMREGFDKP
KDFTLTRDII QVKSVRYRML EDGFGYVRIA QFQEKTDDDL VKALKALEDE AKKPLSGLVL
DLRNDPGGLL DQAVRVADHF VSEGLIVYTE GREKDAKMQF SARKGAKEPN YPIVILINGG
SASASEIVAG ALQDHKRAII MGTQSFGKGS VQTIIPLADE SGLRLTTARY FTPNGRSIQA
KGITPDIVVE RLELPRQSDK KEGFNIRERD LENHFQNGDE SEGSTVTDKK DDRKDKQLST
KPEDNLKNDY QVMRALDLLK GWEIFKKIGS SK
//
