ID M7NGV4_9BACL Unreviewed; 485 AA.
AC M7NGV4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Serine protease Do-like HtrA {ECO:0000313|EMBL:EMR06421.1};
DE EC=3.4.21.107 {ECO:0000313|EMBL:EMR06421.1};
GN Name=htrA_2 {ECO:0000313|EMBL:EMR06421.1};
GN ORFNames=C772_01692 {ECO:0000313|EMBL:EMR06421.1};
OS Bhargavaea cecembensis DSE10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Bhargavaea.
OX NCBI_TaxID=1235279 {ECO:0000313|EMBL:EMR06421.1, ECO:0000313|Proteomes:UP000011919};
RN [1] {ECO:0000313|EMBL:EMR06421.1, ECO:0000313|Proteomes:UP000011919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE10 {ECO:0000313|EMBL:EMR06421.1,
RC ECO:0000313|Proteomes:UP000011919};
RX PubMed=23766406;
RA Shivaji S., Ara S., Begum Z., Ruth M., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Bhargavaea cecembensis Strain DSE10T, Isolated
RT from a Deep-Sea Sediment Sample Collected at a Depth of 5,904 m from the
RT Chagos-Laccadive Ridge System in the Indian Ocean.";
RL Genome Announc. 1:e00346-13(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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:EMR06421.1}.
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DR EMBL; AOFT01000007; EMR06421.1; -; Genomic_DNA.
DR RefSeq; WP_008299058.1; NZ_AOFT01000007.1.
DR AlphaFoldDB; M7NGV4; -.
DR STRING; 1235279.C772_01692; -.
DR PATRIC; fig|1235279.3.peg.1689; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000011919; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EMR06421.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:EMR06421.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011919};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 101..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 387..441
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 50811 MW; 05D9C789CFB8D24F CRC64;
MTNHQNGREP GDQHDPINEP NHNPAEPDIR EQEWQHGEDG VPDQIPDERL TEPARFSTEE
SPEETREEAY RSDMPGAAEE PSAPVQARDS REKKKRGGAG WLQAIGGGVA GSVLTMAIAV
PLLDGDPAET NEPAESGLQS ESQQSTGEVT KVSTDGSLAD MVEQVSGSIV GIVNYQQQQQ
RNPFGGAGSG QSIPAGTGSG VIIKKNDESA YIVTNNHVVE GASKLEVSLE NGERAEAELV
GADALSDLAV VRVDANLVDA EPLAFGDSDA LRAGDSVVAI GNPLGLELSR SVTEGIVSAT
DRSISVDTSA GEWEMNVIQT DAAINQGNSG GALVNMNGEV IGINSLKIGG SGVEGLGFAI
PSNDVVPLVE EMMESGHVER PYAGISMYDV AQIPRGYLEG LPNDISQGVY IAGVDPEGAA
AKGGIKEGDV ITAIDGEEIE DGQALRRYLY SELEVGDQAV FTVYREGKKT EVPVTLGSNK
ASSPS
//
