ID C3X7I2_OXAFO Unreviewed; 488 AA.
AC C3X7I2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN Name=mucD {ECO:0000313|EMBL:EEO29158.1};
GN ORFNames=OFBG_00186 {ECO:0000313|EMBL:EEO29158.1};
OS Oxalobacter formigenes OXCC13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Oxalobacter.
OX NCBI_TaxID=556269 {ECO:0000313|EMBL:EEO29158.1, ECO:0000313|Proteomes:UP000005089};
RN [1] {ECO:0000313|EMBL:EEO29158.1, ECO:0000313|Proteomes:UP000005089}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OXCC13 {ECO:0000313|EMBL:EEO29158.1,
RC ECO:0000313|Proteomes:UP000005089};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Allison M.J., Lander E., Nusbaum C., Galagan J.,
RA Birren B.;
RT "The Genome Sequence of Oxalobacter formigenes OXCC13.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Might be efficient in the degradation of transiently
CC denatured and unfolded proteins which accumulate in the periplasm
CC following stress conditions. {ECO:0000256|ARBA:ARBA00002610}.
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DR EMBL; GG658170; EEO29158.1; -; Genomic_DNA.
DR AlphaFoldDB; C3X7I2; -.
DR STRING; 847.BRW83_2092; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_4; -.
DR Proteomes; UP000005089; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
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 NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 2.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEO29158.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EEO29158.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005089};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 272..363
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 127
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 157
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 228
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 488 AA; 52441 MW; F5943E319FCFE657 CRC64;
MAIMQKTVIF FARRFLLVFL TVGFISFPLM PGEAAPATMV NGLPDLTSLV EKVGPAVVNI
RTIEKIQSRR NPAMDMDRDF QEYLFRFFGI PAPDGQLSGT QPQEQVRRGM GSGFIITADG
YILTNHHVID NADEVFVRLT DNREFKAKII GSDKRTDVAL LKIEGKNLPV LKTGNSANIK
VGEWVLAIGS PFALENTVTA GIISAKARDT GDYLPLIQTD VAVNPGNSGG PLINMAGEAI
GINSQIYSRS GGYMGISFAI PIDEALRVSE QLKKTGKVTR GQIGIQVAEV SVETAKAMNL
PNDRGVMVAR VEKGSAAEKA GVEAGDIILK FNSQSIEKLS ELPRLVGDSI PGTKVSLTVL
RKGKSLVLPV TISKAELDKP ARKDESSSSR QGESLSSSIL GLQVADLTAP QKKRLGINHG
VVVTASASPA FESGIRKGDI ILRLNNGDVT SQQDFQNQLV KAGKAKMVVL LVARNNLIRY
VPVKPVAK
//
