ID A0A2U2AF21_9GAMM Unreviewed; 401 AA.
AC A0A2U2AF21;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Protease SohB {ECO:0000313|EMBL:PWD81169.1};
GN ORFNames=DC083_04560 {ECO:0000313|EMBL:PWD81169.1};
OS Ignatzschineria ureiclastica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC Ignatzschineriaceae; Ignatzschineria.
OX NCBI_TaxID=472582 {ECO:0000313|EMBL:PWD81169.1, ECO:0000313|Proteomes:UP000245020};
RN [1] {ECO:0000313|Proteomes:UP000245020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22644 {ECO:0000313|Proteomes:UP000245020};
RA Tsang C.C., Tang J.Y.M., Fong J.Y.H., Kinne J., Lee H.H., Joseph M.,
RA Jose S., Schuster R.K., Tang Y., Sivakumar S., Chen J.H.K., Teng J.L.L.,
RA Lau S.K.P., Wernery U., Woo P.C.Y.;
RT "Ignatzschineria dubaiensis sp. nov., isolated from necrotic foot tissues
RT of dromedaries (Camelus dromedarius) and associated maggots in Dubai,
RT United Arab Emirates.";
RL Submitted (MAY-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:PWD81169.1}.
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DR EMBL; QEWQ01000003; PWD81169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2AF21; -.
DR OrthoDB; 5614232at2; -.
DR Proteomes; UP000245020; 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; 2.
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:PWD81169.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:PWD81169.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245020};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..94
FT /note="Peptidase S49 N-terminal proteobacteria"
FT /evidence="ECO:0000259|Pfam:PF08496"
FT DOMAIN 127..221
FT /note="Peptidase S49 N-terminal proteobacteria"
FT /evidence="ECO:0000259|Pfam:PF08496"
FT DOMAIN 225..370
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 63..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 45010 MW; 00DA38F9963A6D59 CRC64;
MIYLIDFILF LAKTATLLVG FIAVILFLAS LRNANSGNSG GKIEFKDLGD RFTQIEEGFL
EFSKQDSEEN DQSDVSKNKK SDNADSADKV ENKQEADHAL DRDRSVESEQ STQSTQSTQS
TQSTQSTQSN QSIKATKTAK ETKPKRFWQF WKKEEEESVE PKSKTLYVLE FDGDVHAEEV
KNLREEVSAL LHIAKPEDEV LVKLTSPGGA VNSYGLAASQ LVRIRDKGLK LTVSVDEVAA
SGGYLMACVA NHIVAAPFAI VGSIGVVAAM PNFHKVLKKY NVDYEQFTAG EYKRTVTMFG
ENTDEAKEKF TEELVAIHKV FKNFVQQYRP ELDIEAIATG EYWLAVKGLE LKLVDELKTS
DAYILDAIED YNVYSIKYVE KTTVRQGLSR FLTRIMKRIP F
//
