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Database: UniProt
Entry: A6GLX0_9BURK
LinkDB: A6GLX0_9BURK
Original site: A6GLX0_9BURK 
ID   A6GLX0_9BURK            Unreviewed;       660 AA.
AC   A6GLX0;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Peptidase S8 and S53, subtilisin, kexin, sedolisin {ECO:0000313|EMBL:EDM85001.1};
GN   ORFNames=LMED105_05612 {ECO:0000313|EMBL:EDM85001.1};
OS   Limnobacter sp. MED105.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Limnobacter.
OX   NCBI_TaxID=391597 {ECO:0000313|EMBL:EDM85001.1, ECO:0000313|Proteomes:UP000010322};
RN   [1] {ECO:0000313|EMBL:EDM85001.1, ECO:0000313|Proteomes:UP000010322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED105 {ECO:0000313|EMBL:EDM85001.1,
RC   ECO:0000313|Proteomes:UP000010322};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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:EDM85001.1}.
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DR   EMBL; ABCT01000001; EDM85001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6GLX0; -.
DR   STRING; 391597.LMED105_05612; -.
DR   Proteomes; UP000010322; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07496; Peptidases_S8_13; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR034176; Peptidases_S8_13.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000010322};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        634..653
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          152..458
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   REGION          185..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..626
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        234
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        423
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   660 AA;  66369 MW;  F16BAD4AC0AFC913 CRC64;
     MCIFGFAQLA NVHANPLTAP VTTTATPTPM RWVVNMGDQA QGTAPAGMLQ TLQNTLGVSV
     RMVRPLLQPN SYLVEMQSLP VLGSLQTPQA IRAALQALPG VRFASPDIQL QRTAVPAPND
     GAYSVNQASY MHTGAYASLR MQDVWEQTRG SSNVVIAVLD SGVLFENPEL KGRLLPGYDF
     VSNVTPPTGT RENGTVFDSG SNDGNGRDPD PSDPGDAPPP GFNCPDGSTT SSWHGTTVAS
     VAAAQSNNGQ FLAGMDWNAK VLPVRVSGRC GIATSSDIVD AFYWATGSGR VDPTIGVNPN
     PANIINLSFA TDTPLFGGGC AANDMVALAI ADARARNVSV VVSAGNNSGG AVQYPANCAG
     TIAAGAAEQD GQLANYTARG AGTGFVTLHA PGNSSGLYVG ASNTGGSTPN ANGSTAFLFA
     GTSFSAPMVA GAISLLKAIR PSLTPSQVDS LLSNNALAYP ANASNASGLF GRLECTPTSC
     GVGLLNVLGA VQAARSLANP LPVANVQQSA VVAGNGPFVL DAALSSNSAG GSSNLTFSWQ
     QVFGNPVVLA GTSTSALQVQ SGLAGNIAEF ALTVTDTATN RSNTSVVRLA NSAVNERTFT
     PSSTGGGSGS STGGSGTGTS TPAPVAASSG GGGGGGALGL TGLLGMLMLF GVWRQRPGVA
//
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