ID D9TDT5_MICAI Unreviewed; 1116 AA.
AC D9TDT5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Peptidase S8 and S53 subtilisin kexin sedolisin {ECO:0000313|EMBL:ADL48818.1};
GN OrderedLocusNames=Micau_5312 {ECO:0000313|EMBL:ADL48818.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL48818.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL48818.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP002162; ADL48818.1; -; Genomic_DNA.
DR AlphaFoldDB; D9TDT5; -.
DR STRING; 644283.Micau_5312; -.
DR MEROPS; S08.069; -.
DR KEGG; mau:Micau_5312; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_007528_0_0_11; -.
DR OrthoDB; 5167143at2; -.
DR Proteomes; UP000001908; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.650; -; 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; IPR014756; Ig_E-set.
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; IPR017297; Peptidase_S8A_DPH-A.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PIRSF; PIRSF037854; Dihydropyridine_esterase; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF81296; E set domains; 1.
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};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1116
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003129033"
FT DOMAIN 226..489
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 267
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 442
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1116 AA; 117453 MW; 7981D9D562086439 CRC64;
MLRNRRKMTA LGLGLALALG LPVPALAAAP TAPTGPSAPT GPSAQPGAGP VTVTLITGDR
VTVASGGRAA VRPGAGRANI QFLVGRERDR LTVMPQDALP LVRAGKLDRR LFDVSGLIEA
GYDDARRGSV PLLVTYRPGV ARRTAAPLAG ARVTRDLPAI AGAAVVADKG DTGALWKAVS
ADRSGARLDA AGGVDRIWLD GRRRLTLDHS VPQIGAPTAW AAGWTGKGVR VAVLDTGVDL
SHPDLAGKVA ESRNFTEEAD PDDIVGHGTH VASTIAGSGA ASGGKYRGVA PDATLLSGKV
CEVYGCTESA ILAGMQWAAA EQHATVVNMS LSGGDTPEVD PLEQAVGTLT EQHGTLFVIS
AGNDGADGSV GSPATADAAL AVGAVDRDDV LADFSSRGPR VGDGAIKPDI TAPGVEIVAA
RAAHGQIGDP VGDRYASLSG TSMAAPHVAG AVALLAQQHP GWTPERYKAT LMASAKPHPE
QTAFQQGAGR VDVARAITQQ VTSEPASVSF GVATWPHTDD KPISRTVTYR NGGTAPLTLD
LSTEFTGPGG RTAPAGMLTL STSRLTVPAG DSAQVTVVID TRLGGADGYW TGRLLARAGD
AVVVTPLAVD REVESYDLTV THRNRSGALT DGYYTVLLGL DDGTYRDVYG TGGETRIRVP
KGRYGVQSLI FVDGDQGWSE VSFLAQPELV VAGNQRLALD ARRAKPIRTT VPQRGAAPLL
IDLTAAWGFG DYYNSFGLWT DRFEGLYSAQ IGRTVSDKVF VGALASQWVE PTAPERSPYF
YGLNDLFPGR FPTGFVRHYR PADLATVTNR FAAGYAGMDN ELVVYAERDY NMGGSAIVLP
VQVPGKRIDH LSVTRTRWSA ELAFGERAEE GWLEPRAALE RVPTRYRAGH SYRDEWNKAP
FGPSFPQPQW PEQGITRTGD TVIVSLPVHS DAAGHPGGSL NDTEHTRLYR NGKLVDESPY
PGYGEFTVPP GTANYRLETS ATRGFADLST EVSASWTFRS KRVPGDVPAR LPAMAVRFTP
PLAADSSAPA GRTFTVPVTV QRQPGAPSGR VVALTVDVSY DGGKTWQKAA LKKQGGAWTA
TVRHPAGPGY ASLRATARDD AGNTVTQRII QAYRLR
//
