ID A5FY46_ACICJ Unreviewed; 508 AA.
AC A5FY46;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
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=Acry_1317 {ECO:0000313|EMBL:ABQ30528.1};
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163 {ECO:0000313|EMBL:ABQ30528.1, ECO:0000313|Proteomes:UP000000245};
RN [1] {ECO:0000313|EMBL:ABQ30528.1, ECO:0000313|Proteomes:UP000000245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5 {ECO:0000313|EMBL:ABQ30528.1,
RC ECO:0000313|Proteomes:UP000000245};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) 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; CP000697; ABQ30528.1; -; Genomic_DNA.
DR RefSeq; WP_011942157.1; NC_009484.1.
DR AlphaFoldDB; A5FY46; -.
DR STRING; 349163.Acry_1317; -.
DR KEGG; acr:Acry_1317; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR Proteomes; UP000000245; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:ABQ30528.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABQ30528.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000245};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..508
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039162620"
FT DOMAIN 290..348
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 408..476
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 234
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 508 AA; 52655 MW; 7003C345E99933EF CRC64;
MKLFLARRRP GQLAALTAVM LAGGTLAAIS LDSAFANDKA FDATSKVQKD FKPIPSFAPL
VKDVSPAVVS VTVHLKVQQA DNTQAQNGMP PGMPFAFPFP FPQPQQPQAV EAKGSGFFIS
SDGYIVTNNH VVKNAKSVFV TLSDGSKLPA KIVGTDPSTD LAVLKVKRDK PFPYLQLGDS
AKVVPGQWVI AIGNPFGLAE TVTTGVVSAL GRDIGDGQYD SFIQIDAPIN EGNSGGPLLN
QRGEVIGVNT AILTPSGGSV GIGFSIPSDM VRRIADELIK SGHVTRGFIG VQVQTITPEM
AQAMGVPVHD GRADGALIAE TMPNGPAAKA GLKPGDIITK VDGKMVRDPR ELALAISGIK
PDGKASITYL RGGASHELNL RVEKMPANAE AAFAPGGSQS GPAMHKPELG LSLAPLSDAA
RQQLNLPDNV SGALIAHVAP NSPADEAGLR SGDVIVGVGS MTVNNPDQAV AAIRKAEAAK
AKAIALRVMR GNQALFVAVP LPKEKAGK
//
