ID A0A1D7NPK0_9SPHN Unreviewed; 632 AA.
AC A0A1D7NPK0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Protease-4 {ECO:0000313|EMBL:AOL95690.1};
GN ORFNames=BG023_112783 {ECO:0000313|EMBL:AOL95690.1};
OS Porphyrobacter sp. LM 6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1896196 {ECO:0000313|EMBL:AOL95690.1, ECO:0000313|Proteomes:UP000094080};
RN [1] {ECO:0000313|EMBL:AOL95690.1, ECO:0000313|Proteomes:UP000094080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM 6 {ECO:0000313|EMBL:AOL95690.1,
RC ECO:0000313|Proteomes:UP000094080};
RA Hentchel K., Vargas G., Fiebig A., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; CP017113; AOL95690.1; -; Genomic_DNA.
DR RefSeq; WP_069310935.1; NZ_CP017113.1.
DR AlphaFoldDB; A0A1D7NPK0; -.
DR STRING; 1896196.BG023_112783; -.
DR KEGG; porl:BG023_112783; -.
DR PATRIC; fig|1896196.3.peg.2760; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000094080; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd07018; S49_SppA_67K_type; 1.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004634; Pept_S49_pIV.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047217; S49_SppA_67K_type_N.
DR InterPro; IPR047272; S49_SppA_C.
DR NCBIfam; TIGR00705; SppA_67K; 1.
DR NCBIfam; TIGR00706; SppA_dom; 1.
DR PANTHER; PTHR33209; PROTEASE 4; 1.
DR PANTHER; PTHR33209:SF1; SERINE PROTEASE SPPA, CHLOROPLASTIC; 1.
DR Pfam; PF01343; Peptidase_S49; 2.
DR PIRSF; PIRSF001217; Protease_4_SppA; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AOL95690.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 126..279
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 378..528
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 193
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 394
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 632 AA; 67190 MW; DD19D9AEA50CB9A7 CRC64;
MSFVGKVWKV LVGIKDGLVL LFMLLFFVAL FGILSARPNS GKVRDGALLI ELDGTVVEEK
SLVDPISALL SGTAPVQEYR ARDIIRALDA AATDDRVRAV VFDLTTFLGG GQVHLTEIGE
AMERVRKAKK PVLTYALAYA DDHLLLSSHA SEVWLDPQGL AIISGPGGSN LYYAGLLEKL
SVNARIYRAG DFKSAVEPYS RSSMSDEARQ NVGGLYGALW EEWQANVKKA RPKLAVTRVT
SDPVGWINAS GGDLAKAALE GGLVDKLGDR AQFGARVAEM AGEDPWSNKP GAFASSDLTA
YLADAGQSRA GKAIGVITIA GEIVDGEAGP GVAGGKRIAD VLDEALDDDL GALVVRVDSP
GGSVTASEEI RRAIQRYRDR KIPVAVSFGN VAASGGYWVS MSSDRIFAQP ETITGSIGVF
AVVPTFEKTA ARIGVNADGF RTTPLSGQPD FIGGFSPEMD AIMQSTIAGT YKDFLALVSR
GRRMPVERVD AIGGGRVWDG GTARQIGLVD EFGGLEDALA WAAAKAGAKD GEWHAVYLGE
QMDNYDSLIR QLLTDRAGEA SAALSGDIFA LTARRNDDLM TRMTRDAERL LGVRGVQAVC
LTCPGVAPSR ARPASLMREG QLPGWLAWLA LR
//
