ID A0A1Y2S7P5_9GAMM Unreviewed; 348 AA.
AC A0A1Y2S7P5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Protease SohB {ECO:0000313|EMBL:OTA14656.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:OTA14656.1};
GN ORFNames=Xvie_03487 {ECO:0000313|EMBL:OTA14656.1};
OS Xenorhabdus vietnamensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351656 {ECO:0000313|EMBL:OTA14656.1, ECO:0000313|Proteomes:UP000194350};
RN [1] {ECO:0000313|EMBL:OTA14656.1, ECO:0000313|Proteomes:UP000194350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22392 {ECO:0000313|EMBL:OTA14656.1,
RC ECO:0000313|Proteomes:UP000194350};
RA Tobias N.J., Wolff H., Djahanschiri B., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Systematic genetic and metabolomic analysis of Xenorhabdus and
RT Photorhabdus spp., highlights the requirements for a dual symbiotic and
RT pathogenic life style.";
RL Submitted (OCT-2016) 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:OTA14656.1}.
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DR EMBL; MUBJ01000025; OTA14656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2S7P5; -.
DR STRING; 351656.Xvie_03487; -.
DR OrthoDB; 5614232at2; -.
DR Proteomes; UP000194350; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR002142; Peptidase_S49.
DR InterPro; IPR013703; Peptidase_S49_N_proteobac.
DR InterPro; IPR047272; S49_SppA_C.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF1; PROTEASE SOHB-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR Pfam; PF08496; Peptidase_S49_N; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000313|EMBL:OTA14656.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OTA14656.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..157
FT /note="Peptidase S49 N-terminal proteobacteria"
FT /evidence="ECO:0000259|Pfam:PF08496"
FT DOMAIN 160..301
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 348 AA; 39332 MW; B1F83B2485F42290 CRC64;
MEYLSLYGLF LAKVLTVVLA VVVLVVVCIG LGVRKTMHKG ELKLINLGES YKEKQRQMQQ
ARMSEVEQKI WQKAFKKQQK SDDKQKRAEA KTGQKGLQKP NLYVLDFKGS MDAHEVDSLR
EEISAILAVA DKNDEVLLRL ESPGGVVHGY GLAASQLARL RQKGVRLTVA VDKVAASGGY
MMACVADRII AAPFAIIGSI GVVAQLPNIH RLLKKNDIDV ELHTAGEYKR TLTVLGENTE
QGRKKFQEDL NETHQLFKSF IHQHRPSLDV EKVATGEYWY GTQAKENGLI DEMGVSDDFL
IEKIKHYEVI GVNYSRRKRV IECFMGSAME NVDKLFMRWW QRGEKPLL
//