ID A0A1G6EPN8_9FLAO Unreviewed; 533 AA.
AC A0A1G6EPN8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SDB59473.1};
GN ORFNames=SAMN03097699_2412 {ECO:0000313|EMBL:SDB59473.1};
OS Flavobacteriaceae bacterium MAR_2010_188.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250295 {ECO:0000313|EMBL:SDB59473.1, ECO:0000313|Proteomes:UP000199442};
RN [1] {ECO:0000313|EMBL:SDB59473.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2010_188 {ECO:0000313|EMBL:SDB59473.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; LT629302; SDB59473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6EPN8; -.
DR STRING; 1250295.SAMN03097699_2412; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000199442; Chromosome i.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:SDB59473.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199442};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 89..159
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 533 AA; 60171 MW; 9C47611F832F7272 CRC64;
MPLKKKYIPL LTGIAVAAGV LIGGKLNFTD NNDRLFSTNS KKDKLNRLID YIDYEYVDEV
NTDSIVDVTV NGILENLDPH STYIPKDQLA RVTENMRGDF IGIGISFYTY NDTIAVIRSV
EGGPSEKVGI LPGDRIIMAD GDTIYGKQWT NQQIIQRLKG KKNSKVDLTV YRKGEAELLH
FTVKRSEVPL KSVDAHYMLT ENLGYIKINR FAESTYKEFK EALDNLQEQG ATQLALDLRD
NPGGFVGIAE QIADEFLEDK KLMLFTQNKK GKIEKSFATA KGDFEDGELY ILINENSASA
SEIVAGALQD NDKGIIVGRR SFGKGLVQRE MDLGDGSAVR LTVARYFTPT GRSIQRPYSN
GGNKEYYNDY YQRKSNGELN NESNITVADS LRYETPKGKI VYGGGGIIPD VFVPLDSSRR
NETINYIRRN GYISFFVFEE LDRERAIYKD VALDDFIENF TISDNIILRF QDYINEREGT
KITFVAYHDE IRLLIKAALA RQLFSDEAAE EIMNESDVMI DEVIMLSQAS FPH
//
