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Database: UniProt
Entry: A0A099KJ44_9GAMM
LinkDB: A0A099KJ44_9GAMM
Original site: A0A099KJ44_9GAMM 
ID   A0A099KJ44_9GAMM        Unreviewed;       791 AA.
AC   A0A099KJ44;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Subtilisin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ND16A_1980 {ECO:0000313|EMBL:KGJ90250.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ90250.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGJ90250.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGJ90250.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-2014) 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   -!- 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:KGJ90250.1}.
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DR   EMBL; JQDZ01000104; KGJ90250.1; -; Genomic_DNA.
DR   RefSeq; WP_033078599.1; NZ_JQDZ01000104.1.
DR   AlphaFoldDB; A0A099KJ44; -.
DR   STRING; 1535422.ND16A_1980; -.
DR   PATRIC; fig|1535422.3.peg.3058; -.
DR   eggNOG; COG1404; Bacteria.
DR   OrthoDB; 9790784at2; -.
DR   Proteomes; UP000029848; 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; cd04817; PA_VapT_like; 1.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR   Gene3D; 2.60.120.380; -; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
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; PF02225; PA; 1.
DR   Pfam; PF00082; Peptidase_S8; 2.
DR   Pfam; PF04151; PPC; 2.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029848};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..791
FT                   /note="Subtilisin"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001948431"
FT   DOMAIN          161..394
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          395..480
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          491..553
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   DOMAIN          599..664
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   DOMAIN          708..776
FT                   /note="Peptidase C-terminal archaeal/bacterial"
FT                   /evidence="ECO:0000259|Pfam:PF04151"
FT   ACT_SITE        169
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        202
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        505
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   791 AA;  82826 MW;  0E276873DB684B24 CRC64;
     MKANRLTPKR LLLSTLALSV MTATSMTQAS ELREVSQINE PSETITFAQW QSKQQQQRLD
     KTDRLIVKFK DKHQGKSIPP GLAKKAGLAL KHEKILKNGH HIISFGQQKN MKDVKALINK
     LKNHKSIEFI EPDHKRFLMA QNQPWGISNT QSDLLSDNDA SNMTVCIIDS GYQQDNPDLS
     ANNATGTNNS GTGNWYQNGG SHGTHVAGTI AAVNNSEGVV GIMPNTNVNL HIVKVFNESG
     WGYTGELVDA VDTCVNNGAQ VINMSLGGAG SSNTEKNALQ AAADAGILLV AASGNDGNST
     MSYPASYDAV MAVGAVDQNG QHAEFSQYTS QVEIAAPGEA ILSTVAGDGR LGYITIGGTT
     YGNDEVVPQT RYVQSGSNYV VTNVNGSASG VLASCTISGS SYSCSNVAGN ICLAERNDNQ
     VGSNYPEINP AKACTDAGAA GVIVYSDSAR PGLQNPFLVD GSSDVNVPTV SINRSLAQQL
     LSQLGSNVEL TVNDGQNYAY YNGTSMATPH VTGVAALAWS NNPSCTADDV RSALKSTAID
     LETAGRDDKT GFGLAQAKAA SDLLAAGCGT TTPPPTGGNV LENGVAKTNL TANSSEELSF
     TIEVPAGSTD LSFDMSGGTG DADLYVKFGS APTSSSYDCR PYQSGNSESC PINNVQTGTY
     YVNVIAYSTF SGVSLTANYT ESSTGGTGGA TGGSATVSDI SVARRAWQYY TIDVPAGMAT
     LDFTMSGGTG DADMYIKQGA QPSSSSYDCR PYESGNNEFC SFNNPAATTW HIGIYGYRAA
     SGVNLDVSYN P
//
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