(data stored in ACNUC7421 zone)

SWISSPROT: B4STG6_STRM5

ID   B4STG6_STRM5            Unreviewed;       498 AA.
AC   B4STG6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   SubName: Full=Carboxyl-terminal protease {ECO:0000313|EMBL:ACF50009.1};
DE            EC=3.4.21.102 {ECO:0000313|EMBL:ACF50009.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0304 {ECO:0000313|EMBL:ACF50009.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50009.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50009.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50009.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S41A family.
CC       {ECO:0000256|RuleBase:RU004404}.
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DR   EMBL; CP001111; ACF50009.1; -; Genomic_DNA.
DR   RefSeq; WP_012509830.1; NC_011071.1.
DR   STRING; 391008.Smal_0304; -.
DR   EnsemblBacteria; ACF50009; ACF50009; Smal_0304.
DR   KEGG; smt:Smal_0304; -.
DR   eggNOG; ENOG4105CN1; Bacteria.
DR   eggNOG; COG0793; LUCA.
DR   HOGENOM; HOG000038764; -.
DR   KO; K03797; -.
DR   OMA; TFNQVDW; -.
DR   OrthoDB; 1646508at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01595-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd07560; Peptidase_S41_CPP; 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   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF03572; Peptidase_S41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00245; TSPc; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   TIGRFAMs; TIGR00225; prc; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STG6.
DR   SWISS-2DPAGE; B4STG6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|RuleBase:RU004404,
KW   ECO:0000313|EMBL:ACF50009.1};
KW   Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:ACF50009.1};
KW   Serine protease {ECO:0000256|RuleBase:RU004404};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    498       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002826402.
FT   DOMAIN       98    179       PDZ. {ECO:0000259|PROSITE:PS50106}.
SQ   SEQUENCE   498 AA;  51854 MW;  DE61941D4035863F CRC64;
     MRAARTATLL LALLPALSWA QQTAPAPSQE TSGQAANSEE AVTSKVPLED IRRFVAVYNA
     VRAAYVDPVD DKKLMQSAVR GLLLDLDPHS TYFNKEDAQA FDEQASGAYE GIGVELQQQP
     DNASMKVISP IDDTPAAKAG ILAGDLIIAI DGKPISKIDA SEPLRGAAGS KVVLTIVREG
     KPKPFDVSLT RQTIRVTSVR SRLLEPGYGY IRLSTFQADT GSDFQKHVQQ LQKQSGGQLK
     GLVLDLRSNP GGLLTAAVQV ADDLLDKGNI VSTRGRISIS DARFDATPGD LLKGAPVVVL
     VDAGSASASE VLAGALRDNK RARVVGSRTF GKGSVQTVLP LDNGDSVKLT TARYYTPSGK
     SIQATGIVPE VELKPAATPV EDALPASLSD YSEATLPGHL RGDDEGTEGY HAGAVLPGDG
     PINDALAELK NPGSVAARLK AEAAKAAAAK GAKAAAAKPE ATPDAKAEPK AESKPEAKPE
     AKPEAKPEAK PAPAPAKP
//

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