ID A0A0U5FZ88_9PROT Unreviewed; 502 AA.
AC A0A0U5FZ88;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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:CUW41426.1};
GN ORFNames=XM1_4367 {ECO:0000313|EMBL:CUW41426.1};
OS Magnetospirillum sp. XM-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1663591 {ECO:0000313|EMBL:CUW41426.1, ECO:0000313|Proteomes:UP000063191};
RN [1] {ECO:0000313|Proteomes:UP000063191}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wang Y.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; LN997848; CUW41426.1; -; Genomic_DNA.
DR RefSeq; WP_068436637.1; NZ_LN997848.1.
DR AlphaFoldDB; A0A0U5FZ88; -.
DR STRING; 1663591.XM1_4367; -.
DR KEGG; magx:XM1_4367; -.
DR PATRIC; fig|1663591.3.peg.4312; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000063191; Chromosome I.
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, ECO:0000313|EMBL:CUW41426.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CUW41426.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 270..337
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 405..460
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 58..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 226
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 502 AA; 52875 MW; E2837F57DB50B0A8 CRC64;
MFIARRDKSL AAARLMVGAL AIVALLLPGL AAAAAPPGGF ADLAERLLPA VVNISTTQTL
KGNQGGPEMP QFPPGSPLEE FFKEFMERQQ GARPDAPARK ATSLGSGFII DAAGYIVTNN
HVIADADEIS VKLHDDTVFQ ATLVGRDPKV DLALLKIEPG KKPLTPVPFG NSDEARVGDW
VLAIGNPFGF GGTVTAGIVS ARARDINAGP YDDFLQTDAA INRGNSGGPM FNMRGEVIGI
NSAIISPSGG SIGIGFAVPA SLAVPVLDDL RKFGKVRRGW LGIRIQSLDS DMAENIGLPD
QKGALVAKVD PNGPGVKAGL KDGDVVLKFD GKDITEMRRL PRYVASTPIG KKVEVVIWRD
GKRQTITAAV GEMPEDPAEQ QVKGKPEAPK PQAGKEGVLA IPGAGLTVSS LTPALRERFG
VDDEAKGVIV TEVKPDGPAA EKGMRPGDLI IEADHKPVRS PADLAKQIED GRKAGAKSLL
LRVENPQQLR YIALPLAEGK KK
//
