ID A0A0M4L454_9GAMM Unreviewed; 473 AA.
AC A0A0M4L454;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:ALE01908.1};
GN ORFNames=W908_04620 {ECO:0000313|EMBL:ALE01908.1};
OS Candidatus Pseudothioglobus singularis PS1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE01908.1, ECO:0000313|Proteomes:UP000068905};
RN [1] {ECO:0000313|EMBL:ALE01908.1, ECO:0000313|Proteomes:UP000068905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000313|EMBL:ALE01908.1,
RC ECO:0000313|Proteomes:UP000068905};
RX PubMed=26494659;
RA Marshall K.T., Morris R.M.;
RT "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL Genome Announc. 3:e01155-e01115(2015).
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006911; ALE01908.1; -; Genomic_DNA.
DR RefSeq; WP_053820116.1; NZ_CP006911.1.
DR AlphaFoldDB; A0A0M4L454; -.
DR STRING; 1125411.W908_04620; -.
DR KEGG; tsn:W908_04620; -.
DR PATRIC; fig|1125411.7.peg.906; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000068905; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000068905};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..473
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005797344"
FT DOMAIN 89..161
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 372..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 51471 MW; 2E11712EE1A500F1 CRC64;
MINLKTFFKS FALSVFILFA TSTVADDDNY SPLDSPSFFE GLNTFTAVFS QIKQMYVDDI
DDETLFNNAI RGLIEGLDPH SSFLEPVAQS KVSESTMGKF GGLGIVIGTK GDFIEVVSPI
DDTPAYRAGL KAGDIILQIG DQNVSQINLE EGVKLMRGAP GTTIKLTIGR PEIAPFVVEI
TREVITITSA KGLIVSDGIG YLRIAQFQRP TAEVVEKIIA NLVRKNEGDL DSLIIDLRNN
PGGLLDSSID ISNLFIDEPG IVVYTEGRTP TSNMSFPTKP GDILNGAPIV VLMNVGSASA
SEIVAGALQD HKRAIIMGEE SFGKGSVQSM MSLQDGYGLK LTTARYFTPS GRSIQAKGIS
PDIALDNISL KDEDEEEESI DFSSQEKDLK NALSAQDEDE TNTDDMSDSD STEVDTSDSQ
DEVNPTELTA EEILESQDKI AAERDQEYID LLLEDYYVHE AVNVLKALKI YNK
//
