ID A0A1I6RQS2_9BACL Unreviewed; 376 AA.
AC A0A1I6RQS2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Subtilase family protein {ECO:0000313|EMBL:SFS66986.1};
GN ORFNames=SAMN05444972_105296 {ECO:0000313|EMBL:SFS66986.1};
OS Marininema halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Marininema.
OX NCBI_TaxID=1155944 {ECO:0000313|EMBL:SFS66986.1, ECO:0000313|Proteomes:UP000198660};
RN [1] {ECO:0000313|EMBL:SFS66986.1, ECO:0000313|Proteomes:UP000198660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45789 {ECO:0000313|EMBL:SFS66986.1,
RC ECO:0000313|Proteomes:UP000198660};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FPAA01000005; SFS66986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6RQS2; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000198660; 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; cd07477; Peptidases_S8_Subtilisin_subset; 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; 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; IPR034202; Subtilisin_Carlsberg-like.
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; 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}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 119..346
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 313
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 376 AA; 41114 MW; D778AB0C2F3D14EA CRC64;
MTKPDWLPGT LPMFNRRPRV RKIFHLKGYR SPNFCLREMN RCGGRPVRVL PQLGVVIGEF
YGEDGLYSLE GHPDVAYWEP DSRVTITDPY IGEVSENTDR LPWGVKRIDA HKVWRYTKGR
NVNVAVIDTG IASDHPAVRD NYKGGINILS PMFTPHDYNG HGTHVAGTIA GRAEDLLGVA
PRVNLYAVKA FNRKGSANLS DLLSAINWCI ENKMNVVNMS FGMARVSDTL GQAIRTAYQK
GLVMVAAAGN QGTSGEIDYP ARFSETIGVT ATDRGGEIAS FSNTGPGVDI AAPGDKVSSA
WLNRGTREMS GTSMAVPHVA GTAALLLYLR SELTPDQIRK ILMDSTVSIS HNSDVGLLNA
HRSVQLLARY MGRYVP
//
