ID F1YRM8_9PROT Unreviewed; 542 AA.
AC F1YRM8;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=degP {ECO:0000313|EMBL:EGE48468.1};
GN ORFNames=APO_0562 {ECO:0000313|EMBL:EGE48468.1};
OS Acetobacter pomorum DM001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=945681 {ECO:0000313|EMBL:EGE48468.1, ECO:0000313|Proteomes:UP000018454};
RN [1] {ECO:0000313|EMBL:EGE48468.1, ECO:0000313|Proteomes:UP000018454}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DM001 {ECO:0000313|EMBL:EGE48468.1,
RC ECO:0000313|Proteomes:UP000018454};
RX PubMed=22053049; DOI=10.1126/science.1212782;
RA Shin S.C., Kim S.H., You H., Kim B., Kim A.C., Lee K.A., Yoon J.H.,
RA Ryu J.H., Lee W.J.;
RT "Drosophila microbiome modulates host developmental and metabolic
RT homeostasis via insulin signaling.";
RL Science 334:670-674(2011).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGE48468.1}.
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DR EMBL; AEUP01000014; EGE48468.1; -; Genomic_DNA.
DR AlphaFoldDB; F1YRM8; -.
DR Proteomes; UP000018454; 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; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EGE48468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018454};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 328..375
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 437..515
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 521..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 257
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 542 AA; 55641 MW; 914C90A92129D4BC CRC64;
MFGPSGNCPV GIKQGTVEVV MSGKSVTKVW ARNRRRNWLS ALLASCVLVT AAAPWCSTPA
RAEADSVIKP NTPTSQRIPD FVSLVKQVKP AVVSITSMIR ADAVEGDGGG MGGMPFPFPF
PFQMMPQPSH QTIEARGSGF VISADGYVVT NNHVVKGATK VTVTLDDGTT LPAKVVGRDG
KTDLALLKVT TSEKLPFIEL GESDDVQPGE WVIAVGNPYG LGGTVTAGIV SARGRDINEG
PYDNFIQVDA PINRGNSGGP LFTQDGKVVG VNTAILSPSG GGSIGIGFAI PSDTVRNVVE
QLRKTGHVVR GYLGVNAQVI SPVMARALGL PAPSTPGAPP VGALVASVSP GSPAEKVGLK
SEDVITDFNG QKVSNPHDLA VRVASMAPGK QATIGYLRGG KAQTATVTIG DLKTASSDGS
SGSNTDVARG QRLGIALAPL SRDVRQQLGL SADVRGVVVS DVDPGSPADQ AGIRPGDVIQ
AIGSQAVDSP RAAVASVKAA LASKKPVLLR VMRDNQSLFI AISPDGSNNA PSSDDGGDDD
DN
//
