ID B4SBG0_PELPB Unreviewed; 498 AA.
AC B4SBG0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:ACF44014.1};
DE EC=1.3.1.74 {ECO:0000313|EMBL:ACF44014.1};
DE Flags: Precursor;
GN OrderedLocusNames=Ppha_1782 {ECO:0000313|EMBL:ACF44014.1};
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925 {ECO:0000313|EMBL:ACF44014.1, ECO:0000313|Proteomes:UP000002724};
RN [1] {ECO:0000313|EMBL:ACF44014.1, ECO:0000313|Proteomes:UP000002724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1 {ECO:0000313|Proteomes:UP000002724};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP001110; ACF44014.1; -; Genomic_DNA.
DR AlphaFoldDB; B4SBG0; -.
DR STRING; 324925.Ppha_1782; -.
DR KEGG; pph:Ppha_1782; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_10; -.
DR Proteomes; UP000002724; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0032440; F:2-alkenal reductase [NAD(P)+] activity; IEA:UniProtKB-EC.
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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Oxidoreductase {ECO:0000313|EMBL:ACF44014.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ACF44014.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002724};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 285..351
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 135
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 498 AA; 53033 MW; 7BECD63246310A16 CRC64;
MKYLLLVFAG IAVGALVFSN VEFSLSSRGL SFSNSPSFAT AKNNIENYPI QSLKGFNEAF
VQIAESATPS VVTIFTEKTV NQRIGSPFGF WGRPFFDDFF DMPEIAPRNG QKKVLQGIGS
GVVVTADGYI LTNNHVIDNA DAVYIRTFDN KKIDAKVIGK DSKTDLAVIK VNAKNLKPIL
IGDSDKLRVG EWVIAIGSPL GENFARTVTQ GIVSAKGRAN VGLADYEDFI QTDAAINPGN
SGGPLVNING ELVGINTAIA SRTGGFDGIG FAVPSNMAQK VMTALITTGK VTRGYLGVSI
QDIDENIAKA MHLKAGEGAL VGTVVEGGPA AKIGIKTGDV ILDINDQKVT GSIELRNAIS
SQLPGSMVKF RVLRNGTIML FQARLEEQPA RGVASAMTEE QEKIPAVLGF KAEELTARLA
QKLNLVPGSG KVVLTALDPA SNAYLAGLRV GDIILTLNRQ SVNSFAGYSA LIKNIKSGDL
LFLLVERKGN KIYFAFNV
//