ID C6XIM4_HIRBI Unreviewed; 519 AA.
AC C6XIM4;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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=Hbal_1277 {ECO:0000313|EMBL:ACT58969.1};
OS Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hirschia.
OX NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT58969.1, ECO:0000313|Proteomes:UP000002745};
RN [1] {ECO:0000313|Proteomes:UP000002745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC {ECO:0000313|Proteomes:UP000002745};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP001678; ACT58969.1; -; Genomic_DNA.
DR RefSeq; WP_015827119.1; NC_012982.1.
DR AlphaFoldDB; C6XIM4; -.
DR STRING; 582402.Hbal_1277; -.
DR KEGG; hba:Hbal_1277; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000002745; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ACT58969.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 289..355
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 95..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 519 AA; 54625 MW; 12F66F3996F82C58 CRC64;
MKTTGKSRTL KMSLAMALLG SAAVGGLILS PVGSKIADAK PIVVQAPVGA PLSFADLIEK
VNPAVVTVQV TTEIEAPEQY GELFERFRNI PGFDDFMDRQ GRGEGEEGES EEDEGPAPRE
GRSLGSGFFI SDTGYIVTNN HVVENASEVT ITLSNGDELE AEIIGLDELT DLAVLKVKEG
GKYPYVEFEL GAPPRVGDWV VAVGNPFGLG GTATAGIVSA ISREMNGSNY SNYIQVDASI
NRGNSGGPTF DLYGKVIGVN TAIYSPSGGS VGIGFAIEST VAKEITDILI KDGKVTRGWL
GVSIQSMTVE MAESQGLKNE KGALVADVQV GSPAEKGGIE RGDVILSVNG LAVKDSRELT
RLVGGLIAES KNEFKLIRDG KEKTVSVTVG VRPSDVDSAF NRGGSESEGE KEDEVAPEGA
LVHGLTVKPL SKPEFELFGL KENENGVLVL DLNRNSAFAE AGIAKGDALL EAQGTTLKSA
DDLASVIKNA KKEGKKNILV AVRKGRATIF LPVEIEDLK
//
