ID Q1G7S6_LACDA Unreviewed; 427 AA.
AC Q1G7S6;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=HtrA-like serine protease {ECO:0000313|EMBL:CAI96980.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:CAI96980.1};
GN Name=htrA {ECO:0000313|EMBL:CAI96980.1};
GN OrderedLocusNames=Ldb0140 {ECO:0000313|EMBL:CAI96980.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI96980.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI96980.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CR954253; CAI96980.1; -; Genomic_DNA.
DR RefSeq; WP_011543524.1; NZ_JQAV01000016.1.
DR AlphaFoldDB; Q1G7S6; -.
DR STRING; 390333.Ldb0140; -.
DR MEROPS; S01.447; -.
DR KEGG; ldb:Ldb0140; -.
DR PATRIC; fig|390333.13.peg.782; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_2_9; -.
DR BioCyc; LDEL390333:LDB_RS00570-MONOMER; -.
DR Proteomes; UP000001259; Chromosome.
DR GO; GO:0016020; C: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; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAI96980.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAI96980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001259};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..414
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 49..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 427 AA; 43788 MW; 7C09611568469F32 CRC64;
MSEEQDKQRN TRKKENNRLL TKAAIIGVVA GILGGGIAYG GLSAANLNSN TSSSTASSSS
SNTGENGSVT TSSSGTTKVN KSKTTSGTMT SAYKKVQNAV VSVLNYKYTS SSSSSSDIYS
MFGYGDSDSS DSSSSKKSLT LYSEGSGVIY TTANGKGYIV TNNHVISGAA KVKVILASGK
TIAAKVVGKD STSDLAVLSI DSKYVTQTAS FGDSRSLLSG QTVIAIGSPE GSEYASTVTQ
GIISSPSRTI TYNSNQMTVI QTDAAINSGN SGGPLVNSDG QVIGINSMKL SSSSSGDSVE
GMGFAIPSNE VVTIVNQLVK KGKITRPQLG IKVAAIADLN SYYKKQLGIS TSLKKGLYVA
SVTSGSAAAS AGIKKGDVIT AADGKTVNDV ATLHSILYSH NVGDKVKITV NRNGKTMTFT
VTLQASN
//
