ID W4S7U3_9XANT Unreviewed; 633 AA.
AC W4S7U3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Protease IV {ECO:0000313|EMBL:GAE52596.1};
GN Name=sppA {ECO:0000313|EMBL:GAE52596.1};
GN ORFNames=XPU_4128 {ECO:0000313|EMBL:GAE52596.1};
OS Xanthomonas arboricola pv. pruni str. MAFF 311562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1414836 {ECO:0000313|EMBL:GAE52596.1, ECO:0000313|Proteomes:UP000019143};
RN [1] {ECO:0000313|EMBL:GAE52596.1, ECO:0000313|Proteomes:UP000019143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311562 {ECO:0000313|Proteomes:UP000019143};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) 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:GAE52596.1}.
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DR EMBL; BAVB01000365; GAE52596.1; -; Genomic_DNA.
DR AlphaFoldDB; W4S7U3; -.
DR Proteomes; UP000019143; 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, ECO:0000313|EMBL:GAE52596.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 142..297
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT DOMAIN 400..551
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT ACT_SITE 211
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
FT ACT_SITE 417
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001217-1"
SQ SEQUENCE 633 AA; 68157 MW; 7EDFDAEB61D9B4F4 CRC64;
MNHPVHRSPI ASFFVGLWDV MNFTRRLIFN LVFFGFLFLV LLLFVVAIAR GDGSKPLAER
TTLVINPEGT LVEQFSADPV SRSLAKAVGD KSAEEVQLRD LVRVIEAAGK DRKIERVVLN
LDKFQPAGFA SQREVAAALQ KLRASGKQIV AFSESMSQGQ YLLAAQANEV YLDPMGSVLL
EGLGRYRQYF REGLQDKLGV DVHLFRVGEY KSAAEPYILD AASADAKEAD LFWMNDVWQR
YLADVGKARK LSPAQLTAGI DTLPEGVAAA GGDLAKFALQ QKLVDGLKTR EDVDALLTKR
GVADSDADSG FRNIGFNDYL SKLQAQRSPM DSRPQVAVVV AAGEISGGEQ PAGRIGGEST
AALLRQARDD DEVKAVVLRV DSPGGEVFAS EQIRREVVAL KQAGKPVVVS MGDLAASGGY
WISMNADRIY ADPSTISGSI GIFGMVPNLT RALDKIGVHT DGVGTTRFAG AFDITRPLDP
AAGQVIQAVI NKGYADFTGK VAQARHQSVD AIDKVARGRV WSGAQARQHG LVDAFGGMSE
AVADAADRAK LSRGKFRVRY VEKPATPFSQ FMSGFAGSRM GAWMLGDSGM ARALLARSLP
KVDTQLRFVE DAVHDSKAGG TPVKSLAYCF CGF
//
