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Database: UniProt
Entry: D0LUE6_HALO1
LinkDB: D0LUE6_HALO1
Original site: D0LUE6_HALO1 
ID   D0LUE6_HALO1            Unreviewed;       591 AA.
AC   D0LUE6;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Protease-like protein {ECO:0000313|EMBL:ACY19269.1};
GN   OrderedLocusNames=Hoch_6805 {ECO:0000313|EMBL:ACY19269.1};
OS   Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC   Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX   NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY19269.1, ECO:0000313|Proteomes:UP000001880};
RN   [1] {ECO:0000313|EMBL:ACY19269.1, ECO:0000313|Proteomes:UP000001880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC   {ECO:0000313|Proteomes:UP000001880};
RX   PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA   Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA   Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA   Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL   Stand. Genomic Sci. 2:96-106(2010).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; CP001804; ACY19269.1; -; Genomic_DNA.
DR   RefSeq; WP_012831861.1; NC_013440.1.
DR   AlphaFoldDB; D0LUE6; -.
DR   STRING; 502025.Hoch_6805; -.
DR   KEGG; hoh:Hoch_6805; -.
DR   eggNOG; COG4934; Bacteria.
DR   HOGENOM; CLU_461364_0_0_7; -.
DR   OMA; FPTEMQA; -.
DR   OrthoDB; 5478896at2; -.
DR   Proteomes; UP000001880; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; 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; cd04056; Peptidases_S53; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR015366; S53_propep.
DR   InterPro; IPR030400; Sedolisin_dom.
DR   PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 1.
DR   PANTHER; PTHR14218:SF15; TRIPEPTIDYL-PEPTIDASE 1; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF09286; Pro-kuma_activ; 1.
DR   SMART; SM00944; Pro-kuma_activ; 1.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51695; SEDOLISIN; 1.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000313|EMBL:ACY19269.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000313|EMBL:ACY19269.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT   DOMAIN          170..591
FT                   /note="Peptidase S53"
FT                   /evidence="ECO:0000259|PROSITE:PS51695"
SQ   SEQUENCE   591 AA;  64000 MW;  80906273E69E0565 CRC64;
     MNEVGNNVLT VVFNEKGAAD IYGLALRVSD PGSSDYGKYV SRSTLKQMAA PSHTARQRCE
     EWFEQHNMHI FERPTPQIIL AEATDEELNK AFGPDYSAWL KGASSGGAPR GLWGLPTEIA
     GVIKAIHLHT VDSPGELSLL SHGIPSARTP DTMDDAERAP VASEEGVPQS VGGFSVADVR
     QIYEFPDDWD GSGETIALLN LAGRPSVQDL QAFWRANGVE RADPEHVLIG GARDEHQGFV
     ARLEATMGAA WIGAMAPGAR LVIYDINPEM VADPWATMVA VAVADTEREP SILVSTWTTP
     ETDYYRDNGS RVFSDLMRQA TALGITMVVA SGDWGVYSGR PNVRRGHRKA VAAAWPQGVF
     PAVEDQVLAV GGTMITSREP LTEVAWSGPL PPNRTLRESM PFRLFATSGG FSEQVPLPVW
     QNKHIPYSRA FSRGANLPAV TPYGRGYPDV ALMAAGPAVQ LMPGAQLSSV GYQLVMDGRW
     INYAGGTSMS APVWATIIAC MNQARRAKGK SRLGFVNPLL YDLAKKLQAT PEKNPFRDIT
     SGNSDVILDA VFQEGIAQRY CLHGYDAQGD WDPVTGLGVP RVDRLIELIS S
//
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