ID A0A060R835_9BACT Unreviewed; 542 AA.
AC A0A060R835;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative carboxy-terminal processing protease {ECO:0000313|EMBL:CDN31540.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:CDN31540.1};
GN ORFNames=BN938_1453 {ECO:0000313|EMBL:CDN31540.1};
OS Mucinivorans hirudinis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC Mucinivorans.
OX NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN31540.1, ECO:0000313|Proteomes:UP000027616};
RN [1] {ECO:0000313|EMBL:CDN31540.1, ECO:0000313|Proteomes:UP000027616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3 {ECO:0000313|Proteomes:UP000027616};
RX PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA Nelson M.C., Bomar L., Graf J.;
RT "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT hirudinis M3T.";
RL Genome Announc. 3:e01530-e01514(2015).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; HG934468; CDN31540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060R835; -.
DR STRING; 1433126.BN938_1453; -.
DR KEGG; rbc:BN938_1453; -.
DR PATRIC; fig|1433126.3.peg.1438; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_2_0_10; -.
DR Proteomes; UP000027616; Chromosome I.
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; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:CDN31540.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:CDN31540.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027616};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 70..146
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT COILED 465..533
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 542 AA; 61031 MW; BF9461B6CE259503 CRC64;
MRRLFLLILL APALAWGQGE AKWDYRLGKS MEELMAVFRE ANLYYVDSTN PERMLKAAAK
AMLSGLDPYT VYLSDDDMAD FETLITGKYA GVGAMIRQKG DWVEISEPKR GTPSDKAGLK
AGDRLLYIND TDLKGLGSEK VSSLLRGEPG TFFVLKYRPL ADTAKTKEVT IKRETITQPS
VPYFGYAADS VGYIRFDSFT EDCSKEVREA IVQLGEGGMK ALILDLTSNG GGSVGEAINI
ASFFLPRGSE VVSLRGKIKE MDAKYTTKNA PIEPTIPLAV LMGRESASAS EILAGALQDL
DRAVIIGERS FGKGLVQSPR QIGSNSILKV TTAKYYTPSG RCIQALDYTH RREDGSVDSI
PEVMRKVFTT KNGRIVKDGG GIDPDIYISP EFLANFTGLL LAYGYLEDFA NQYAAHNTHS
KEFRVTDALY DDFIEFMRHK EMRYESATAV KFEELRQWAE REKYAERLTE EFAAIERKIK
EDKIKELNTF SKEIKNVLEN EIIRRWYYEW GAIERSLEQN KEVKRAVEIL EDKAEYEKLL
GR
//
