ID A0A1M5MHT0_9FLAO Unreviewed; 541 AA.
AC A0A1M5MHT0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SHG76984.1};
GN ORFNames=SAMN04488116_2463 {ECO:0000313|EMBL:SHG76984.1};
OS Allomuricauda flava.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=570519 {ECO:0000313|EMBL:SHG76984.1, ECO:0000313|Proteomes:UP000184532};
RN [1] {ECO:0000313|Proteomes:UP000184532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22638 {ECO:0000313|Proteomes:UP000184532};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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; FQWL01000003; SHG76984.1; -; Genomic_DNA.
DR RefSeq; WP_073179937.1; NZ_FQWL01000003.1.
DR AlphaFoldDB; A0A1M5MHT0; -.
DR STRING; 570519.SAMN04488116_2463; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000184532; Unassembled WGS sequence.
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; 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:SHG76984.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 90..160
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 541 AA; 61495 MW; 0B4E08337B4856D6 CRC64;
MKKKYQYIVP TLLAFVLAVG IFIGGKLHFD DSPEKLFSTN SKKDKLNRLI DYIDYEYVDD
IDTDSIVDVT VNNILGKLDP HSVYIPRSEM EEVSENMKGD FVGIGISFYM YRDTITVIRT
IKNGPSHKSG IKAGDRILIA DKDTLFGRRI ANNEIVSTLK GKIGTKVDLK VFRKSDNRTL
DVTVTRDRVP IRSVDSYYML TSDMGYIKIN RFAESTFGEF KDALRKLKLR GAEKLVLDLR
DNPGGYLGIA EKLADEFLED DKLILFTKNK KGRVKKAFAT KKGDFEDKPV YVLINERSAS
ASEIIAGALQ DNDIGTIVGR RSFGKGLVQR EMDLGDGSAV RLTVSRYYTP TGRSIQRSYK
KGHRDYYQTF MERYRNGEMV SVDSIKVADS LKFVTPGGKI VYGGGGIIPD VFVPIGTNEE
EAVESMDGAE FFSRFVFEHL EQDRTRYSYL SKNEFLDDFR VDDILFDEFI QFVLNRKISL
DFYEQEDKIK DFLKANIAEQ LFSPNLSAQI KGEHDAMLDK VKELDQDIFN QAEVGAIKLK
D
//
