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Database: UniProt
Entry: A0A495AFC0_9ENTR
LinkDB: A0A495AFC0_9ENTR
Original site: A0A495AFC0_9ENTR 
ID   A0A495AFC0_9ENTR        Unreviewed;       349 AA.
AC   A0A495AFC0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Protease SohB {ECO:0000313|EMBL:RKQ38718.1};
GN   Name=sohB {ECO:0000313|EMBL:RKQ38718.1};
GN   ORFNames=D8M09_15960 {ECO:0000313|EMBL:RKQ38718.1};
OS   Enterobacter sp. R1(2018).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=2447891 {ECO:0000313|EMBL:RKQ38718.1, ECO:0000313|Proteomes:UP000271976};
RN   [1] {ECO:0000313|EMBL:RKQ38718.1, ECO:0000313|Proteomes:UP000271976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1(2018) {ECO:0000313|Proteomes:UP000271976};
RA   Ontanon O.M., Ghio S., Rivarola M., Campos E.;
RT   "Enterobacter sp. from a bacterial cellulose degrading consortium draft
RT   genome.";
RL   Submitted (OCT-2018) 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:RKQ38718.1}.
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DR   EMBL; RCAA01000050; RKQ38718.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495AFC0; -.
DR   OrthoDB; 5614232at2; -.
DR   Proteomes; UP000271976; 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:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RKQ38718.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:RKQ38718.1};
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..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..158
FT                   /note="Peptidase S49 N-terminal proteobacteria"
FT                   /evidence="ECO:0000259|Pfam:PF08496"
FT   DOMAIN          162..309
FT                   /note="Peptidase S49"
FT                   /evidence="ECO:0000259|Pfam:PF01343"
SQ   SEQUENCE   349 AA;  39561 MW;  035FDB798C091E5F CRC64;
     MDFIANYGLF LAKIVTVVVA IAAIVTIVVN VAQRKKHHHG ELRLTNLSEQ YQEMREEMQV
     ARLDDHQQKL WHKGQKKKHK LEAKQAKARA RRGETTSSDK PTLYVLDFKG SMDAHEVTSL
     REEITAVLAV IKPEDEVLLR LESPGGVVHG YGLAASQLQR LREHKVRLTV AVDKVAASGG
     YMMACVADRI VAAPFSIIGS IGVVAQVPNF HRLLKRNDID VELHTAGQYK RTLTLFGENT
     EQGREKFRED LNETHHLFKH FVHEMRPALD IDAVATGEHW YGVQAKEKGL VDEVSTSDDL
     LIGLMKNHEV IGVRFTRRKK MMERFTGSAA NSLDRLLLRW WQRGEKPLL
//
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