ID A0A1H9I1Q2_9GAMM Unreviewed; 358 AA.
AC A0A1H9I1Q2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Serine protease SohB {ECO:0000313|EMBL:SEQ68468.1};
GN ORFNames=SAMN03080615_02368 {ECO:0000313|EMBL:SEQ68468.1};
OS Amphritea atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Amphritea.
OX NCBI_TaxID=355243 {ECO:0000313|EMBL:SEQ68468.1, ECO:0000313|Proteomes:UP000198749};
RN [1] {ECO:0000313|Proteomes:UP000198749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18887 {ECO:0000313|Proteomes:UP000198749};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; FOGB01000006; SEQ68468.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9I1Q2; -.
DR STRING; 355243.SAMN03080615_02368; -.
DR OrthoDB; 5614232at2; -.
DR Proteomes; UP000198749; 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:SEQ68468.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SEQ68468.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..164
FT /note="Peptidase S49 N-terminal proteobacteria"
FT /evidence="ECO:0000259|Pfam:PF08496"
FT DOMAIN 167..316
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 81..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 40204 MW; CD1B244E7B6666D3 CRC64;
MVDFLASYGL FLAKALTVVG AIILVIVAIG AVASRNKRDS KEGYLSIHSM NETLEDMEHA
LKEVVLDSEV YKQQLKAEEK QEKQEAKARK KALKKTKSQP DAEPERKRVF VLDFDGDIKA
SELEPMREEI TAVLTMATEK DEVVIRLESP GGMVHSYGLA SSQLERIKQR GVPLTVCVDK
VAASGGYMMA CLADKIVAAP FSILGSIGVV AQLPNFHRLL KKHDIDYEVL TAGEYKRTLT
VMGENTEKGR QKFIEDLEDT HSLFKEFVGE FRPQVDLEKV ATGEVWFGRR ALEVNLIDEI
STSDEYLTQA CEDADVYTVR YEYKKTLQDR LSDMSIKTTD TLFTKWAGRI LNSHLLAK
//
