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Database: UniProt
Entry: C3M8N0_SINFN
LinkDB: C3M8N0_SINFN
Original site: C3M8N0_SINFN 
ID   C3M8N0_SINFN            Unreviewed;       521 AA.
AC   C3M8N0;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 93.
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   OrderedLocusNames=NGR_c07830 {ECO:0000313|EMBL:ACP24576.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24576.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24576.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Acts on substrates that are at least partially unfolded. The
CC         cleavage site P1 residue is normally between a pair of hydrophobic
CC         residues, such as Val-|-Val.; EC=3.4.21.107;
CC         Evidence={ECO:0000256|ARBA:ARBA00001772};
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DR   EMBL; CP001389; ACP24576.1; -; Genomic_DNA.
DR   RefSeq; WP_012707361.1; NC_012587.1.
DR   RefSeq; YP_002825329.1; NC_012587.1.
DR   AlphaFoldDB; C3M8N0; -.
DR   STRING; 394.NGR_c07830; -.
DR   MEROPS; S01.274; -.
DR   KEGG; rhi:NGR_c07830; -.
DR   PATRIC; fig|394.7.peg.3597; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000001054; Chromosome.
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; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACP24576.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ACP24576.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          317..371
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          418..493
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          104..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..133
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        186
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        261
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ   SEQUENCE   521 AA;  54671 MW;  2731382640477988 CRC64;
     MSMIKTPRPS LKTVLKTSTV AGLAAVMLTT GLPAQITQSF AEAVKVQAPS VPSFANVVDA
     VSPAVVSVRV QAREQASNDE SNFTFDFGGR GFEDLPDDHP LKRFFREFGG PDSRDGDRAD
     RWRDRRGPRG EGRLRPRAQG SGFFITEDGY LVTNNHVVSD GSAFTVIMND GTELDAKLVG
     KDSRTDLAVL KVDSANRKFT HVSFADDKNV RVGDWVVAVG NPFGLGGTVT AGIVSARGRD
     IGSGPYDDYL QVDAAVNRGN SGGPTFNLSG EVVGINTAIF SPSGGNVGIA FAIPASVAKD
     VVDSLIKDGS VSRGWLGVQI QPVTKDIAES LGLSEASGAL VVEPQAGSPG EKAGIKKGDI
     VTALNGEPVK DPRDLARRVA TMRPGATADV TLWRDGKSQS VKLEIGTLPE EAKATTPDTS
     DEQTDQGQAG EEALADLGLA VTPSEDGAGV TIASVDPDSD AADRGLKEGE KIVSVNNQEV
     KSADDILKVI NNAKKDGRSK ALFQIQADEG SRFVALPIAQ S
//
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