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Database: UniProt
Entry: A0A0R2HVM6_CARDV
LinkDB: A0A0R2HVM6_CARDV
Original site: A0A0R2HVM6_CARDV 
ID   A0A0R2HVM6_CARDV        Unreviewed;       477 AA.
AC   A0A0R2HVM6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Membrane serine protease Do {ECO:0000313|EMBL:KRN56738.1};
GN   ORFNames=IV74_GL000738 {ECO:0000313|EMBL:KRN56738.1};
OS   Carnobacterium divergens DSM 20623.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN56738.1, ECO:0000313|Proteomes:UP000051658};
RN   [1] {ECO:0000313|EMBL:KRN56738.1, ECO:0000313|Proteomes:UP000051658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN56738.1,
RC   ECO:0000313|Proteomes:UP000051658};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S1C family.
CC       {ECO:0000256|ARBA:ARBA00010541}.
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:KRN56738.1}.
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DR   EMBL; JQBS01000018; KRN56738.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2HVM6; -.
DR   SMR; A0A0R2HVM6; -.
DR   PATRIC; fig|1449336.4.peg.756; -.
DR   eggNOG; COG0265; Bacteria.
DR   Proteomes; UP000051658; Unassembled WGS sequence.
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};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KRN56738.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051658};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        90..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          362..449
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..84
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..189
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  50217 MW;  D9BEA94309483A63 CRC64;
     MRYDANGNLI PEENNQTEVE KNEFVSSENE AKISQESAAN VSRETQKETP KRATSNSSTT
     GNGGNGGGRP PKEPTTNSPR KSGGSWKSGL IGGLIGGLII ALVGGGLAFS YLPKDNSSVP
     DTTTNKGNVV TSNVKANVTT DTTKAVEQVE DAVVSVANMQ KQNQQGMLGG DYSQSKSNDS
     SNLETTSEGS GVIYKKDGDT AYVVTNNHVI NGSDAVEVIL KDGTKVQAKV IGSDVWTDLA
     VLSIPSEKVK TVATFGDSDS IKVGEPAIAI GSPLGTNFAT SVTQGIISAK NRTVAMDINE
     DGVEDWDMTA IQTDAAINPG NSGGALINIA GQVIGINSMK ISQDTVEGMG FAIPSNDVVK
     IISELEKNGE IVRPVLGVSL RDLSQISAQQ QERVLKLPEK VTEGVVITDV QTNSAAEKAG
     LKQYDTIVEI NGTPVTDNVS LRKVIYNLKV GDKVDVKYYR DGKEATANVT MEASKSL
//
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