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Database: UniProt
Entry: A0A1V3IYQ2_9PAST
LinkDB: A0A1V3IYQ2_9PAST
Original site: A0A1V3IYQ2_9PAST 
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}.
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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
//
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