ID I3CCB8_9GAMM Unreviewed; 484 AA.
AC I3CCB8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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 ORFNames=BegalDRAFT_0341 {ECO:0000313|EMBL:EIJ41261.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41261.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ41261.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41261.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) 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}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; JH600070; EIJ41261.1; -; Genomic_DNA.
DR RefSeq; WP_002683047.1; NZ_JH600070.1.
DR AlphaFoldDB; I3CCB8; -.
DR STRING; 395493.BegalDRAFT_0341; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_6; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000005744; Unassembled WGS sequence.
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:SF130; PERIPLASMIC SERINE ENDOPROTEASE DEGP-LIKE; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF17820; PDZ_6; 1.
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:EIJ41261.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 269..328
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 47..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 220
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 484 AA; 52454 MW; D6A8E22A4A8E55B3 CRC64;
MRKIFVYASF LIGLSMSLLS LGVQSRSLPE FTELVEKYGP AVVNISTTTK KETTPPPTEK
KLPQTIPNLP EDSPFNEFFR RFFEDEENAP YLNELPSTSL GSGFIISADG YVVTNNHVIE
NADEIIVRLT DRREFTAELI GADARTDLAL LKLSATELPF VKLGNANDLK VGEWVLAIGS
PFGFEYSATA GIVSAKGRSL PTDSYVPFIQ TDVAINPGNS GGPLFNLDGE VVGVNSQIYS
RTGGFMGLSF AIPVDVMKNI VDQLREKGKV SRGWLGVLIQ DVTRELAESF GMTRPQGALV
AKVLPNSPAE AAGFQAGDII IEFNGKKIDH SSDLPPIVGV TPINSVIATK IIRAGKEQNL
QVTIAELPAE DDLQKTMTGQ SKVIRNKLGL TLGNLEENQR KELEIAEGGV IVKSAEGIAQ
EAGVRVDDII LMIANTSVKD VAQVEELISN LKSGQAVPIL VKRGSSQLFL ALKMPKEEKK
EEKK
//
