ID G9A4V8_RHIFH Unreviewed; 465 AA.
AC G9A4V8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=SFHH103_01103 {ECO:0000313|EMBL:CCE95602.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE95602.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCE95602.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCE95602.1,
RC ECO:0000313|Proteomes:UP000007735};
RX PubMed=22374952; DOI=10.1128/JB.06729-11;
RA Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA Vinardell J.M., Zehner S., Gottfert M.;
RT "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL J. Bacteriol. 194:1617-1618(2012).
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};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; HE616890; CCE95602.1; -; Genomic_DNA.
DR RefSeq; WP_014328081.1; NC_016812.1.
DR AlphaFoldDB; G9A4V8; -.
DR STRING; 1117943.SFHH103_01103; -.
DR GeneID; 48972709; -.
DR KEGG; sfh:SFHH103_01103; -.
DR PATRIC; fig|380.5.peg.1174; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_5; -.
DR Proteomes; UP000007735; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR041489; PDZ_6.
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; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF17820; PDZ_6; 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:CCE95602.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CCE95602.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..465
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039441540"
FT DOMAIN 250..326
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 354..446
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 107
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 137
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 212
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 465 AA; 49023 MW; 0A5B649B4113EADB CRC64;
MIFGRRALPA LVLAIALSSP AAAQDNKTVP QSHTEMQLSF APLVKQTANA VVNVYAERVV
ERRSVFAGDP FFEEFFGQRM PNRTEKQSSL GSGVVVRRDG IVVTNNHVIE GADDIKVALA
DGREYPCKII LKDDRLDLAV MKIESDGPFD IIPIGDSDAV EVGDLVLAMG NPFGVGQTVT
SGIVSALARN QVSSGDFGFF IQTDAAINPG NSGGGLINMK GELIGINTAI FSRGGGSNGV
GFAIPANLVK VFVASAEGGG GSFIRPFVGA TFEPVTSDVA EALGLDRARG ALVTAVQPGG
PAANAGMKPG QVVTAVNGIS VEHPDALGYR LTTVGIGHEA RVTVAEHGEA HDITLKLERA
PETAPRDERL IEGRNPFAGA VVANLSPRLA DELRMPTSLQ GVVVTEVNRG SPAARIGLEP
KDIVRSVNGT PIDNSKTLES VVAEDASFWR VEIERDGQLI RQFFR
//
