ID S2XB85_9STAP Unreviewed; 255 AA.
AC S2XB85;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Serine protease {ECO:0000256|RuleBase:RU004296};
DE EC=3.4.21.- {ECO:0000256|RuleBase:RU004296};
GN ORFNames=HMPREF1208_01656 {ECO:0000313|EMBL:EPD49308.1};
OS Staphylococcus sp. HGB0015.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1078083 {ECO:0000313|EMBL:EPD49308.1, ECO:0000313|Proteomes:UP000014407};
RN [1] {ECO:0000313|EMBL:EPD49308.1, ECO:0000313|Proteomes:UP000014407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0015 {ECO:0000313|EMBL:EPD49308.1,
RC ECO:0000313|Proteomes:UP000014407};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Staphylococcus sp. HGB0015.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:EPD49308.1}.
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DR EMBL; AGEO01000017; EPD49308.1; -; Genomic_DNA.
DR RefSeq; WP_016425870.1; NZ_KE150418.1.
DR AlphaFoldDB; S2XB85; -.
DR GeneID; 64048143; -.
DR PATRIC; fig|1078083.3.peg.1633; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_073589_1_1_9; -.
DR Proteomes; UP000014407; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR15462; SERINE PROTEASE; 1.
DR PANTHER; PTHR15462:SF8; SERINE PROTEASE; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004296};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004296};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004296};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU004296}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT CHAIN 26..255
FT /note="Serine protease"
FT /evidence="ECO:0000256|RuleBase:RU004296"
FT /id="PRO_5006994076"
FT DOMAIN 33..255
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 82
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 132
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
FT ACT_SITE 210
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR608256-1"
SQ SEQUENCE 255 AA; 28134 MW; 0C7CA4FC9681B71D CRC64;
MKKMIAQTLS VASLLFMTLT QASYAADFTN YNVIDKDTRV RVENTTVKPY QAITFLTMAW
DNDGAACTGS VIGPNKVLTA AHCVYDPKKG GLAKSTTLEP GLNAKYQPYS KFISTHVRVP
QQYIEKQQSD YDIAIIDVQP SAGASIGKVV KPFELETAND FTGKDFEVAG YPSDKFKVFP
GPTMWKDIGV VDRQEGNKAY YTADASHGQS GAPLFDKTTH KLFGVHTSYV KGKNTESNRG
TTLTDEIYNW VKQNL
//