ID A0A0B2A6B8_9MICO Unreviewed; 644 AA.
AC A0A0B2A6B8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase S53 domain-containing protein {ECO:0000259|PROSITE:PS51695};
GN ORFNames=LK09_12540 {ECO:0000313|EMBL:KHK97103.1};
OS Microbacterium mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK97103.1, ECO:0000313|Proteomes:UP000031030};
RN [1] {ECO:0000313|EMBL:KHK97103.1, ECO:0000313|Proteomes:UP000031030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK97103.1,
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:KHK97103.1}.
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DR EMBL; JTDK01000011; KHK97103.1; -; Genomic_DNA.
DR RefSeq; WP_039399889.1; NZ_JTDK01000011.1.
DR AlphaFoldDB; A0A0B2A6B8; -.
DR STRING; 1348253.LK09_12540; -.
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 CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
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.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000031030};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..644
FT /note="Peptidase S53 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002065956"
FT DOMAIN 246..644
FT /note="Peptidase S53"
FT /evidence="ECO:0000259|PROSITE:PS51695"
SQ SEQUENCE 644 AA; 65507 MW; 857103688EF6256F CRC64;
MRKPVLGVSI AVIATVAAAL GGAGAANAAA PTKSPIPNSS PGWLAHGAGV TKGAAAATTG
AVNARVYLAP SGGLAALQAY ATAVSTPGSA QYRHFLTPAQ YHAKFDATAS TVGAVTSWLK
AAGLKTAVEA NHRYVDVTGG VGAANKAFGV TLTKYTHDGI SVQAPSGPAY TPASLAGSVI
AITGLDTTPS TVSPKTQKPA PPSAGYRNAP VCGLTYGAAT PQNLPAPDGT NLPKFMGNDL
PYTPCGYTGP QLRNAYESGV TGGLDGSGVT VAITDAYASP TVLADANAYA KQTGDPQFAN
GQYSESLPNA YVHVNASNGK PQCDMAGWYG EETLDVEAVH AMAPGANIRY YAGKSCNDKD
LLDTFARIND ENRAQIVTNS WGGAGDVVKP ALLLEYQTLF LQGATQGISY LFSSGDDGDE
NARLGSPQTD YPASDPFVTA VGGTSTAITA DGIIGETGWQ TSKYLLKDGA WTLNTSFLYG
GGGGYSSNIP EPQYQKDAGI QSPNGGRAVP DVSMDADPTT GMLIGQTQTF NGVASYGTFR
IGGTSLASPL FAGVTAVKIQ AGGGHGLGLL NPGIYSTKGA GFHDVTGDMP DAGAIRVDFT
NGLDASGGYT YSVRTFNGAE TTLKVGTGWD PSTGWGSARA GWIQ
//
