(data stored in SCRATCH zone)

SWISSPROT: B4STC9_STRM5

ID   B4STC9_STRM5            Unreviewed;       477 AA.
AC   B4STC9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Periplasmic serine endoprotease DegP-like {ECO:0000256|RuleBase:RU364067};
DE            EC=3.4.21.107 {ECO:0000256|RuleBase:RU364067};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0267 {ECO:0000313|EMBL:ACF49972.1};
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:ACF49972.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49972.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49972.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Acts on substrates that are at least partially unfolded.
CC         The cleavage site P1 residue is normally between a pair of
CC         hydrophobic residues, such as Val-|-Val.; EC=3.4.21.107;
CC         Evidence={ECO:0000256|RuleBase:RU364067};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU364067}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|RuleBase:RU364067}.
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DR   EMBL; CP001111; ACF49972.1; -; Genomic_DNA.
DR   RefSeq; WP_012509800.1; NC_011071.1.
DR   STRING; 391008.Smal_0267; -.
DR   EnsemblBacteria; ACF49972; ACF49972; Smal_0267.
DR   KEGG; smt:Smal_0267; -.
DR   eggNOG; ENOG4105C0H; Bacteria.
DR   eggNOG; COG0265; LUCA.
DR   HOGENOM; HOG000223642; -.
DR   OMA; QAQPFEG; -.
DR   OrthoDB; 741829at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01355-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF13180; PDZ_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4STC9.
DR   SWISS-2DPAGE; B4STC9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|RuleBase:RU364067};
KW   Oxidoreductase {ECO:0000313|EMBL:ACF49972.1};
KW   Protease {ECO:0000256|RuleBase:RU364067, ECO:0000313|EMBL:ACF49972.1};
KW   Serine protease {ECO:0000256|RuleBase:RU364067};
KW   Stress response {ECO:0000256|RuleBase:RU364067}.
FT   DOMAIN      276    367       PDZ. {ECO:0000259|PROSITE:PS50106}.
SQ   SEQUENCE   477 AA;  49528 MW;  E1D7AD103BC97F43 CRC64;
     MRPLPTLLTL AIAAAFGGFV ATGLNAHLDN RADAAPLPAV LPTAAALPAS VAGQAVPSLA
     PMLEKAMPAV VSVNTKQVVR VRNPFFNDPF FRRLFPDIPQ ERINESLGSG VIIDAKEGLV
     LTNHHVIDNA DDVQVTLADG RTVKAEFLGS DRDTDIALIR IPAQNLTDIK LGNSDQLRVG
     DFVVAIGNPF GFSQTVTSGI VSAVGRSGIR GLGYQNFIQT DASINPGNSG GALVDLQGQL
     VGINTASFNP QGSMAGNIGL GLAIPSNLAR SVVDQLVKHG VVVRGTLGVE SQNLTAQIAQ
     GLGLGETRGA LVTRVLAGSA AAAAGLKPGD VVVSANGQRV DSAEALHNVE GLATVGSPLT
     LDVRREGKPL QIKAILKEQA RAVTGDSLDP RLGGATFVDL PESLRQSGAG GVLVSEVKRG
     SRAASNGLQQ GDIITDATVG EFADLASWRA NFQQRPPTLV LRVLRNNGQQ QGQLVMR
//

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