ID A0A0L6HUA4_9MICO Unreviewed; 520 AA.
AC A0A0L6HUA4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=AKH00_14095 {ECO:0000313|EMBL:KNY04645.1};
OS Microbacterium sp. GCS4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1692239 {ECO:0000313|EMBL:KNY04645.1, ECO:0000313|Proteomes:UP000037096};
RN [1] {ECO:0000313|Proteomes:UP000037096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCS4 {ECO:0000313|Proteomes:UP000037096};
RA Jones K.J., Moore K., Sambles C., Love J., Studholme D.J., Aves S.J.;
RT "Genome sequencing of alga-associated bacteria.";
RL Submitted (JUL-2015) 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 -!- 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:KNY04645.1}.
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DR EMBL; LGYE01000004; KNY04645.1; -; Genomic_DNA.
DR RefSeq; WP_050723397.1; NZ_LGYE01000004.1.
DR AlphaFoldDB; A0A0L6HUA4; -.
DR STRING; 1692239.AKH00_14095; -.
DR PATRIC; fig|1692239.3.peg.2846; -.
DR OrthoDB; 5177045at2; -.
DR Proteomes; UP000037096; 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 CDD; cd00306; Peptidases_S8_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; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
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; 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};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 209..493
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 154..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 271
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 477
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 520 AA; 55378 MW; 64448CB0A1E05906 CRC64;
MEQPRGWSWQ DRAEGSIRRG TALDPNVEPV EGVRAFPTAY LPERLLITFD RDDDHEAYDG
EVKALRDAAA SFGWELDIES EATRLNAAPL LPGVPGFLRA RLLTPDEAVR GESPVAPDAW
RVLQRARRST RSTMPRTSLE HVVSIDPVGL NPFSRTNPFS RTNPFSRTNP VRGGGSGGSD
DYLEPGRGAR QPVTWVGPAP QRGPAPKRGR RPVVAVLDTG CGVHDWLPDD IVTRQVELDG
VPIGLTDDAD PERYPDLYGQ LDGEIDAVAG HGTFIAGIIR QAAPDADILS VRMAGALGVI
DESTFLTTVA QVVELLRRHR ADPSTGHPID VLNLSLGYYH ETPEDGLFST TLTALLAKAR
ELGCVVVCSA GNDAIDRPSF PASLWPWPGA DNGIVPDKDA PLVSVGALNP SARSVALFSN
VGPWVRVYAP GAAVVSTSPG FVGGEQASTR ADVDGLHRET IDPDDYRGGF AIWSGTSFAA
PYVAGRIAAQ LGAVPPDGVT MKAAATAVDA VLKGLPAPRD
//
