ID A0A1V3IYQ2_9PAST Unreviewed; 352 AA.
AC A0A1V3IYQ2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Protease SohB {ECO:0000313|EMBL:OOF47153.1};
GN ORFNames=BKK52_09925 {ECO:0000313|EMBL:OOF47153.1};
OS Rodentibacter trehalosifermentans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1908263 {ECO:0000313|EMBL:OOF47153.1, ECO:0000313|Proteomes:UP000189161};
RN [1] {ECO:0000313|EMBL:OOF47153.1, ECO:0000313|Proteomes:UP000189161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1987082031 {ECO:0000313|EMBL:OOF47153.1,
RC ECO:0000313|Proteomes:UP000189161};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
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:OOF47153.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MLHL01000057; OOF47153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3IYQ2; -.
DR OrthoDB; 5614232at2; -.
DR Proteomes; UP000189161; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OOF47153.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OOF47153.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189161};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..160
FT /note="Peptidase S49 N-terminal proteobacteria"
FT /evidence="ECO:0000259|Pfam:PF08496"
FT DOMAIN 164..312
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT COILED 63..93
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 352 AA; 39083 MW; 6FD70AB6B3F53894 CRC64;
MWSDILVGYS IFILEILTIL LVIAAIAAFI ISARQQRAGV QGELVITDLS ENFENTVKHL
RNFHLSEEEL KQLEKAEKKA EKQKTKAVKA KLKKGEVAET AKPCIYVLDF KGDISASQTT
ALREEISAIL NVAKPEDEVL LRLESPGGVV HGYGLAASQL SRLTQKGIKL TVAVDKMAAS
GGYMMACVAD KIVAAPFAIV GSIGVVAQIP NIHRLLKKHD VDVDVMTAGE FKRTMTVLGE
NTEKGKQKFQ QELEETHQLF KQFVQQNRPH LDVDKVATGE HWFGSQALEL QLVDAISTSD
DLLLEAMKEK SVVGITYKVK KPLLQKLGQQ AEERMDSLIQ RYIHKNAQDF IH
//