ID A0A0W1DH61_9SPHN Unreviewed; 637 AA.
AC A0A0W1DH61;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Signal peptide peptidase SppA {ECO:0000313|EMBL:KTE17503.1};
GN ORFNames=ATE71_02445 {ECO:0000313|EMBL:KTE17503.1};
OS Sphingopyxis sp. H115.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759073 {ECO:0000313|EMBL:KTE17503.1, ECO:0000313|Proteomes:UP000054021};
RN [1] {ECO:0000313|EMBL:KTE17503.1, ECO:0000313|Proteomes:UP000054021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H115 {ECO:0000313|EMBL:KTE17503.1,
RC ECO:0000313|Proteomes:UP000054021};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTE17503.1}.
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DR EMBL; LNSA01000002; KTE17503.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W1DH61; -.
DR STRING; 1759073.ATE71_02445; -.
DR Proteomes; UP000054021; Unassembled WGS sequence.
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, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 136..287
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 387..538
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 203
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 637 AA; 67229 MW; 1A040AEB3E3E5FF5 CRC64;
MPDGDRPRPT TSFPRKVWNL LVAIKDGLAL IFLLLFFVLL FGLLSGRPNA GLPVNEGALL
IELDGIVSEQ PAEVDTLAAL SGGAQLKEVR VRDVVHALEV AADDKRVTSV VLDLDRFLGG
GQVSLAEIGG AIDKVRAKKK PVLAFATAYT TDSYQVASHA SEIWADSIGG VAIAGPGGSR
LYYKGLMDRL GVTAHIYRVG TFKSAVEPFL RSDQSPEAKE ANLAYASVLW DNWLTDVKRA
RPAAKLDAFI ADTAGAVQAA GNDLSKASLD AGLVDKLGSR MAFNTRVAEI SGAADDSRPW
EYNAIPLENW VAANPPKEKG SAIAVVPVVG EIVDGEAPTG LAGGETVAQH ILDAAADSSI
KAIVLRVDSP GGSVLASEEI RQALLAAKAK KLPIVVSMAN VAASGGYWVS TPADRIFAEP
ETITGSIGVF GILPSFDQAL AKIGVNADGI ATTPLSGQPD VFGGVNDEFN ALAQASVEDI
YARFTGLVAK SRKQPIEKVR TIAEGRVWAG GTARQIGLVD QFGGLPDAMK AAAKLAKVDG
DFHPKYFEDE PSEFSKMLAS WSGAEKETAA LPRGWFGIAA MNRQLTERRL MQDLTMLTQA
GSVQAACLDC RAYLPAVPRP GKAEAKGFLA TLALFLK
//
