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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//