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Database: UniProt
Entry: A0A074K1V5_9RHOB
LinkDB: A0A074K1V5_9RHOB
Original site: A0A074K1V5_9RHOB 
ID   A0A074K1V5_9RHOB        Unreviewed;       908 AA.
AC   A0A074K1V5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE            EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN   ORFNames=DT23_06205 {ECO:0000313|EMBL:KEO55562.1};
OS   Thioclava indica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1353528 {ECO:0000313|EMBL:KEO55562.1, ECO:0000313|Proteomes:UP000027471};
RN   [1] {ECO:0000313|EMBL:KEO55562.1, ECO:0000313|Proteomes:UP000027471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DT23-4 {ECO:0000313|EMBL:KEO55562.1,
RC   ECO:0000313|Proteomes:UP000027471};
RX   PubMed=25361528; DOI=10.1007/s10482-014-0320-3;
RA   Liu Y., Lai Q., Du J., Xu H., Jiang L., Shao Z.;
RT   "Thioclava indica sp. nov., isolated from surface seawater of the Indian
RT   Ocean.";
RL   Antonie Van Leeuwenhoek 107:297-304(2015).
CC   -!- SIMILARITY: Belongs to the peptidase S1B family.
CC       {ECO:0000256|ARBA:ARBA00008764, ECO:0000256|RuleBase:RU004296}.
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:KEO55562.1}.
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DR   EMBL; AUNB01000051; KEO55562.1; -; Genomic_DNA.
DR   RefSeq; WP_051697315.1; NZ_AUNB01000051.1.
DR   AlphaFoldDB; A0A074K1V5; -.
DR   eggNOG; COG2374; Bacteria.
DR   eggNOG; COG3591; Bacteria.
DR   eggNOG; COG4249; Bacteria.
DR   OrthoDB; 500593at2; -.
DR   Proteomes; UP000027471; Unassembled WGS sequence.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR013830; SGNH_hydro.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR36234; LYSYL ENDOPEPTIDASE; 1.
DR   PANTHER; PTHR36234:SF5; LYSYL ENDOPEPTIDASE; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF13472; Lipase_GDSL_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00839; V8PROTEASE.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004296};
KW   Protease {ECO:0000256|RuleBase:RU004296};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027471};
KW   Serine protease {ECO:0000256|RuleBase:RU004296};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          93..291
FT                   /note="SGNH hydrolase-type esterase"
FT                   /evidence="ECO:0000259|Pfam:PF13472"
FT   DOMAIN          634..886
FT                   /note="Endonuclease/exonuclease/phosphatase"
FT                   /evidence="ECO:0000259|Pfam:PF03372"
FT   ACT_SITE        422
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT   ACT_SITE        463
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT   ACT_SITE        534
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
SQ   SEQUENCE   908 AA;  99828 MW;  44D100CC797C6D32 CRC64;
     MTTQITLTEL KAKIRDIDTP DEEIAAYLLA APEASDAFAP QVRINPDLVD DEGTEADVAM
     RFFNAMSKRR RQKKYLRKIE NGWTGLRVVS EGDSWFQYPF LLHDVIDQLF DDYAIYSLGA
     AGDLVQDMLD QDEILQAVRQ HNPHVFLISG GGNDLLGDGM LQTALHPFKT GKLAKDYPNS
     TFTKRLKDII GVYRSIFTTL LAEFPNLKIL CHGYDYAQPA NARWLGKPME ALGIKDKTLQ
     AQIVAELVER FNTALVDLAA EFPGSVVRVS CLNCVGSNWH DELHPNNTGY GAAAGKFRAI
     IDSMFGANAP FEVTAPLSPG KEAKIDAHDL NPEAFRELVD HRGRELLDTP LPPTEDEARR
     KEIEQDISQH FEKISGGADF LPASFLYRGA DAAAAVCRIN LPGGSGTGFM IATRNFIMTN
     NHVIGDEDEA REAVAEFNFE EGGASLMVNL DPDRFFVTST ELDFTIVGCD DPALEIFDPI
     PLLRNPSTVT RGEKVNIVQH PRGRPKEVAL HNNDVLRVKD KVIWYETDTE PGSSGSPVFN
     NTWDLVALHH AGWVEGGVTT NEGVRIAAIV SHLVARQHIE ATASFKLMEL LSTVPDSSPH
     LGFFDIAGIT GSSVQEVEVP EYKGSLEFAD IGFWNIEHFN DAISDTRVDK VACVLGHLSL
     DAMGLVEVQK DAMERLIASL QALGHSYDYK YLDVKGRQDL AVLYDSKTTE VNISAKILNR
     HKTAWAATTE SGRTAFPRRP LIATVKVAPN TEGGDPVEFI MILLHLKAFG DPQSKARRRL
     AAEILTEVIA DIRKTEKLPV VLGGDLNETL NTDVLGPLTD APDLFTLTTD DAADNALSYV
     GARYRSLIDH IVVSNDVHMA PISGDDAAIV RLDKSVADFT RDVSDHVPLV IRMVSRDAPI
     QIGSAGKK
//
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