ID D5UA53_BRAM5 Unreviewed; 489 AA.
AC D5UA53;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:ADG71576.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:ADG71576.1};
GN OrderedLocusNames=Bmur_1489 {ECO:0000313|EMBL:ADG71576.1};
OS Brachyspira murdochii (strain ATCC 51284 / DSM 12563 / 56-150) (Serpulina
OS murdochii).
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=526224 {ECO:0000313|EMBL:ADG71576.1, ECO:0000313|Proteomes:UP000001915};
RN [1] {ECO:0000313|EMBL:ADG71576.1, ECO:0000313|Proteomes:UP000001915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51284 / DSM 12563 / 56-150
RC {ECO:0000313|Proteomes:UP000001915};
RX PubMed=21304710; DOI=10.4056/sigs.831993;
RA Pati A., Sikorski J., Gronow S., Munk C., Lapidus A., Copeland A.,
RA Glavina Del Tio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Brachyspira murdochii type strain (56-150).";
RL Stand. Genomic Sci. 2:260-269(2010).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; CP001959; ADG71576.1; -; Genomic_DNA.
DR RefSeq; WP_013113993.1; NC_014150.1.
DR AlphaFoldDB; D5UA53; -.
DR STRING; 526224.Bmur_1489; -.
DR MEROPS; S41.004; -.
DR KEGG; brm:Bmur_1489; -.
DR eggNOG; COG0793; Bacteria.
DR HOGENOM; CLU_017295_3_0_12; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000001915; 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; 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 Hydrolase {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ADG71576.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ADG71576.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 98..167
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 465..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 54959 MW; 5ECF7AD52C0BEAB5 CRC64;
MIKNKERLLW IFLLIFVAAI SFFNFKSPSL AIAQQGKAQS DNDFYYYSRL FQKVFATLQQ
NFVDTNSVTT KKLMYGAIKG MLEATDDPFT FLLDEELNQA LNTEMSGRYG GVGLSISKNA
DKGLMVVSPI EDGPGEKAGI LSGDIITEID GKSTKDMSVD NAANIMRGKE GTKVTLTIVR
DGVAEPIKYP LTRAIIEIKS VKYKMVDDTV GYIRITTFGD DTARDLEDAL IDLKKQGMKK
LVLDLRNNPG GRLDTAINIV EEFLTEGKIV YTRGRTKNEN QDYYASKKGD EWLEGDMVVL
VNQYSASASE ILSGALQDSG RAKLLGETTF GKFSVQYVLP LDTRDNTSFK FTVAHYYTPN
GRRLHGKGLT PDFVVVEPKL SSTDITALTE LRKGGQISAY AKKYPNESSD AAALPAFKEE
LRNQNIMASD YLLERLIYNE RNLDNYKEIY DLRYDKQLKA AIEYLETGKE PPQDKEEPRE
NWSNEKEEN
//
