ID A0A081P0V7_9BACL Unreviewed; 482 AA.
AC A0A081P0V7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:KEQ24330.1};
GN ORFNames=ET33_08555 {ECO:0000313|EMBL:KEQ24330.1};
OS Paenibacillus tyrfis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ24330.1, ECO:0000313|Proteomes:UP000028123};
RN [1] {ECO:0000313|EMBL:KEQ24330.1, ECO:0000313|Proteomes:UP000028123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSt1 {ECO:0000313|EMBL:KEQ24330.1,
RC ECO:0000313|Proteomes:UP000028123};
RA Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT "Draft genome sequence of Paenibacillus sp. MSt1.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEQ24330.1}.
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DR EMBL; JNVM01000016; KEQ24330.1; -; Genomic_DNA.
DR RefSeq; WP_036685400.1; NZ_JNVM01000016.1.
DR AlphaFoldDB; A0A081P0V7; -.
DR eggNOG; COG0793; Bacteria.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000028123; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
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; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_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; PF07833; Cu_amine_oxidN1; 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; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Protease {ECO:0000313|EMBL:KEQ24330.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028123};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001761209"
FT DOMAIN 89..172
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 482 AA; 51485 MW; 71081470BAD037C6 CRC64;
MNKFKKLPKW RKQTVSAMLA LTLLIPAASP VLAADAKSAA AERITEVLDA LEKNHVSGPK
ADKLSETGIR AMVESLGDPY TQYFTAEQLQ SFEDAVQNQY VGIGVRVGME EEGVYVADVF
AGSPAKEAGM LRGDIIVKVG DAPAAGKKID EVTSKILGPV DTEVRLQVLR DGQTKELTVK
RKKVQIPTVV AKRFQNVGYI EIASFSSDAV ELVSKELSAL KAQGIQSLIV DLRDNPGGLL
ETAQQLARLF VKQGTLIHTR DRNGVDQPVE FANGTTQPFP VFFLVNENSA SASEVLTGAL
QDYGVITAIG TKTFGKGSVQ NVIPLKSGGA IKVTIEEYLT PKLRKVNQVG LEPDKKVEGA
MAQLLTAIRA AGASRLDLTL DRHSATVNGT EVQDSFDVIR ENGQTYVPAR VLAALLGASV
EWNETAKSVQ LVAGDAKTSY TPAAADFVLK NGTGYLNVAQ TAAAFNGLSW KDDGKTLTLG
AN
//
