ID A0A1X3CTS0_9NEIS Unreviewed; 487 AA.
AC A0A1X3CTS0;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OSI11018.1};
GN ORFNames=BWD10_03400 {ECO:0000313|EMBL:OSI11018.1};
OS Neisseria zoodegmatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=326523 {ECO:0000313|EMBL:OSI11018.1, ECO:0000313|Proteomes:UP000193466};
RN [1] {ECO:0000313|EMBL:OSI11018.1, ECO:0000313|Proteomes:UP000193466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21643 {ECO:0000313|EMBL:OSI11018.1,
RC ECO:0000313|Proteomes:UP000193466};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:OSI11018.1}.
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DR EMBL; MTBM01000003; OSI11018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3CTS0; -.
DR STRING; 326523.BWD10_03400; -.
DR Proteomes; UP000193466; Unassembled WGS sequence.
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; 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};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..487
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010863378"
FT DOMAIN 91..173
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 401..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 51829 MW; CFF190AD1547926B CRC64;
MSNSTLKKVA LYTLGALSGV ALSLSVQSYA AGEKNNEALP VQSIRTMAEV YGQIKANYYQ
DKSDEDLIEG AMKGMVAGLD PHSEYMTKKD YADLKESTTG EFGGLGMEVG AEDGFVKVIS
PIEDTPAERA GVKSGDFIVK INGVSTRGMT VNEAVKKMRG KPGTDIVLTL SRKDAAKPIT
VKITRAIIKV KSVRHHLLEP GYGYIRISQF QERTVPALNE SAQALVKQNK GALKGLVLDL
RDDPGGLLNG AVGVSAAFLP ADSTVVSTKG RDGKGGMSLK ATPEDYMLSS GRDPLSGLPA
ELKTIPVTVL INSGSASASE IVAGALQDHR RAVVVGTQSF GKGSVQSVLP LSNGSAIKLT
TSLYYTPKDR SIQAQGIVPD VEVKDKDRLF ESREADLIGH IGNPLGGKEV NGNDYVPSES
LQETPGAKGK KEKAKDEDLS SRRIPNPAKD DQLRKALELV KSPDQWQKSL GLAAKKPAPK
KDNGESK
//
