ID A0A1Q5CP66_9ACTN Unreviewed; 1254 AA.
AC A0A1Q5CP66;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=A6A27_15715 {ECO:0000313|EMBL:OKI85226.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI85226.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI85226.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI85226.1,
RC ECO:0000313|Proteomes:UP000186700};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, 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:OKI85226.1}.
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DR EMBL; LWLS01000013; OKI85226.1; -; Genomic_DNA.
DR RefSeq; WP_073833266.1; NZ_LWLS01000013.1.
DR AlphaFoldDB; A0A1Q5CP66; -.
DR STRING; 1718947.A6A27_15715; -.
DR OrthoDB; 9813435at2; -.
DR Proteomes; UP000186700; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
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 PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 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:UP000186700};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1254
FT /note="Peptidase S8/S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013293186"
FT DOMAIN 229..491
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 238
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 444
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1254 AA; 129410 MW; 45FDD58664CAA2C9 CRC64;
MRRTWRRHTL ASAGILAIAA TALSPSAVGA SAAGESRPIV GSANQAQGQQ SATVTLISGD
RVRVTRTADG QPLAQVLPGV DGTVPDYETL RDGDNLYVFP ATAGQALAAD LVDRELFNVT
GLVAEGFDDS HADAIRLIAQ YDEGNRTVSD TTPAPTGASE SSTLASVNSL SYAVDKSDVT
AAWSELTDAS SGAGRGLAKL WLDRALRASL ADSTAQVGAP AAWTAGLDGK GSKVAVLDTG
VDAGHPDLAG RIGQTKDFTG SKYGTDDKVG HGTHVASTVA GTGAESGGKE RGVAPGAELL
IGKVLDDSGA GYESQIIAGM QWAVANNADV VSMSLGSMRP TTTCDDPIAQ AVNELSGSSR
SLFVIAAGNI GAAQNTVSSP GCATSALTVG AVDSTDATAY FSSRGPVGGT HALKPEIAAP
GVGILAAAAG GRGVYAYRSM SGTSMATPHV AGAAAIAKEA NPTLTGEQLK ELLTSSADPT
VAGAAQEVGA GRLDIARMLS QTVTGQSSVY GGEFAYPQTK GYNSKSLTYA NAGDTPVDLR
LSVEKVTGND SRPVNTPLVR LPQHVIVPAH GTVEVPVTVQ LGANIPDSAL GDITARIVAT
GGGQRVSTAF NLYATAPSVT LTVTVLDRNG NPATGSSSVD IVNTDTSKGE RRFLNGKVQT
YAVRPGHYFL TSFALTPTPG AANPSTPQSL AYLARPEVTI DKDTSIVLDA RQANPLTVST
GQPSELRSTT LTFERQWPTS WLHSGSMSTG PGTREIYAQI TGKVAKGDGS FEFGHWSRRI
TPLVSSMTTS GGLALHPLSP RAGVGNLDGQ GTAEAVSVGA GTAADFKAVD IKGKVAVAHI
PDGSDFSIQT RAASAGAKAL LLYRDDPGTW LAQVGTNAVP LPVYTLSAAE GSSLGSELAA
GPVTLTWSAQ AKSPYAYTLG FFSDGQLVTA QKHDVADASL GRIQATYSSM GATTDFGDMT
AAQRPSTVAF AVGGIDALAV PNTRTEYLTA DGTQWYKSII SSFPFGEVMN DRFRTFAPGQ
VVTDSWYGGS VTPGVRNDND GTPQMIAERQ GDLIGVAPTI WADSAGHWSD GGSFGDLGNM
VLKRNGVTIA TSSYPYDVFT VPSEDATYEL TLNTEKVGAP AKFWKRSTAT RTTWTFSSHK
EPDVYSRPLP MLMPRLDIPA DGFKAVAAGS VAIPARVQAN PGYTAGAIVE AHVWTSTDNG
TTWVEGTTSL TPGGPELVVN HSGDSGKQVS LRVEFTDAEG AKVSQTITRA YDVR
//
