ID A0A1L3ZZ13_9SPHN Unreviewed; 625 AA.
AC A0A1L3ZZ13;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Signal peptide peptidase SppA {ECO:0000313|EMBL:API60867.1};
GN ORFNames=BSL82_00720 {ECO:0000313|EMBL:API60867.1};
OS Tardibacter chloracetimidivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Tardibacter.
OX NCBI_TaxID=1921510 {ECO:0000313|EMBL:API60867.1, ECO:0000313|Proteomes:UP000182063};
RN [1] {ECO:0000313|Proteomes:UP000182063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJ-A5 {ECO:0000313|Proteomes:UP000182063};
RA Lee H., Ka J.-O.;
RT "Complete Genome Sequence of alachlor-degrading Sphingomonas sp. strain JJ-
RT A5.";
RL Submitted (NOV-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; CP018221; API60867.1; -; Genomic_DNA.
DR RefSeq; WP_072598522.1; NZ_CP018221.1.
DR AlphaFoldDB; A0A1L3ZZ13; -.
DR STRING; 1921510.BSL82_00720; -.
DR KEGG; sphj:BSL82_00720; -.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000182063; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000182063};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 125..278
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 379..530
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 396
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 625 AA; 65761 MW; 9B02318501E3B1AC CRC64;
MRLLRLIWRI LVGVKDALVL LFMLLFFGAL YAALAGRAAT VVPSEAALTL DLDGVIVDQP
AEQPPLALLS GGSNLVREIR VRDVVHSVDA AAKDGRIKAL VLDLDRFQGA GPAHLQVIGE
ALKRFRTAGK PIYAYATAYM DPGYYLASYA NEVWMAPLGG VLLTGPGGPN LYFKGLIEKL
AINVEVFRVG AFKSAVEPFT RSDQSPEAEA AAQALVNTIW SVWKGDVARA RPRAKIESYI
DALPQQVAAA GGDLAKAGVA SGLVDKLGSR AEFARMVARL VGRGSDKTAA SWSHVKLADY
ARVARHGAVQ SGPGVGVVYV SGEIVDGEAG PGTAGGDTIA GLIEEALADK NVKALVVRVD
SPGGSVMASE RIRLALMEAR RQNLPVVASM GSVAASGGYW VATSAETIYA QPTTLTGSIG
VFAIIPTFSE TLEKAGIAAD GVRSTPYSGE PDILRGLSPQ VKQLLQLSVE DIYRRFLARV
AVARKMPTAR VDEIGQGRVW AGATARKLGL VDHMGGLDVA VAEAARRAGL DPAKARAIYI
EKSPALPFQI LDDLLMETMP AQSRDPWSGL VASSRGALVR AFDDAQAIAS GPAIQIRCLE
CGIAGGGSQA SNAALVEKLM PVNIR
//
