ID A0A0B1ZZA9_9MICO Unreviewed; 518 AA.
AC A0A0B1ZZA9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase S53 {ECO:0000313|EMBL:KHK96076.1};
GN ORFNames=LK09_17230 {ECO:0000313|EMBL:KHK96076.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK96076.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK96076.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK96076.1,
RC ECO:0000313|Proteomes:UP000031030};
RA Lee L.-H.;
RT "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KHK96076.1}.
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DR EMBL; JTDK01000017; KHK96076.1; -; Genomic_DNA.
DR RefSeq; WP_039402301.1; NZ_JTDK01000017.1.
DR AlphaFoldDB; A0A0B1ZZA9; -.
DR STRING; 1348253.LK09_17230; -.
DR OrthoDB; 3480681at2; -.
DR Proteomes; UP000031030; Unassembled WGS sequence.
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:InterPro.
DR CDD; cd04056; Peptidases_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR PANTHER; PTHR14218:SF42; PEPTIDASE S53 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14218; PROTEASE S8 TRIPEPTIDYL PEPTIDASE I CLN2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031030}.
FT DOMAIN 170..518
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 51759 MW; 5C98F885BAED4284 CRC64;
MTPDIPGGHP LPGSERAPIR GGVPQGAVHP DAPIDATLVL RRRAEVPDDV LANPIPHDEF
VEKYGADPAD AAAVEASVRA AGAEVVSTDL GERLIRIRAK ASVVRELFGV ELNTVALGDS
SYRERTGGLT LPDDLHERVV AVLGLDDRPQ AETHFRVLPT TPTAAASAVS YTPVQVGELY
GFPPGTDGTG RTVAIIELGG GFAQSDLDAY FAGLGIPTPI VTAVGVDGAS NQPGQDPNGA
DGEVLLDIEV VGALAPGAHI VVYFAPNTDA GFVDAVTKAA HASPTPDAIS ISWGQSEDAW
TAQSRSAMDA AFVDAAGMGA TVTAAAGDNG SGDNAGDGAP HVDFPASSPH ALGCGGTALH
GSGSTISSET VWNDGAAGGA TGGGVSDTFP LPSWQGAVGV PPDEAGASGR GVPDVAGNAD
PRTGYQVRVD GTDMVIGGTS AVAPLWAALI ARIVQATGTR MGLAQPKLYA GATASGTSAG
FRDITSGNNG AFAARPGWDA CTGLGSPDGA ALLRALGG
//
