ID A0A109JA79_9BRAD Unreviewed; 455 AA.
AC A0A109JA79;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:KWV45174.1};
GN ORFNames=AS156_24005 {ECO:0000313|EMBL:KWV45174.1};
OS Bradyrhizobium macuxiense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV45174.1, ECO:0000313|Proteomes:UP000057737};
RN [1] {ECO:0000313|EMBL:KWV45174.1, ECO:0000313|Proteomes:UP000057737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR 10303 {ECO:0000313|EMBL:KWV45174.1,
RC ECO:0000313|Proteomes:UP000057737};
RA Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT from nodules of Centrolobium paraense.";
RL Submitted (NOV-2015) 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:KWV45174.1}.
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DR EMBL; LNCU01000126; KWV45174.1; -; Genomic_DNA.
DR RefSeq; WP_066515595.1; NZ_LNCU01000126.1.
DR AlphaFoldDB; A0A109JA79; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000057737; 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; 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 Protease {ECO:0000256|RuleBase:RU004404};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}.
FT DOMAIN 92..160
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 381..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 48797 MW; 923A68BE827C70CD CRC64;
MMRKTSVILL SAATGAALTL FVTQPRAVLM GSSARAATSD TYRQLNLFGD VFERVRSDYV
EKPDDSKLIE SAISGMLSGL DPHSSYMDAK SFRDMQVQTR GEFGGLGIEV TMEDGLIKVV
SPIDDTPASK AGIMANDIIT MLDDEAVQGL TLNQAVEKMR GPVNTKIKLK IIRKGQDNPI
DVTLVRDNIR VRSVRARVEA DDIAYIRITT FNEQTTEGLK KEVANLQSQI GDKLKGYIID
LRNNPGGLLE EAVTVSDSFL ERGEIVSTRG RNAEETQRRT AHPGDLTKGK PVIVLINGGS
ASASEIVAGA LQDHKRATLV GTRSFGKGSV QTIIPLGSGN GALRLTTARY YTPSGKSIQA
KGIVPDIEVL QDVPDELKAR TDTKGEASLR GHLKTNDGDE KTGSQSYVPP DAKDDKALKM
ADDLLHGIKS TSSAPPAAPS DKAAVDKPAN NKAAN
//
