ID Q3JJJ4_BURP1 Unreviewed; 500 AA.
AC Q3JJJ4;
DT 08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Serine metalloprotease {ECO:0000313|EMBL:ABA52421.1};
DE EC=3.4.21.- {ECO:0000313|EMBL:ABA52421.1};
GN OrderedLocusNames=BURPS1710b_A1101 {ECO:0000313|EMBL:ABA52421.1};
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA52421.1, ECO:0000313|Proteomes:UP000002700};
RN [1] {ECO:0000313|EMBL:ABA52421.1, ECO:0000313|Proteomes:UP000002700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b {ECO:0000313|EMBL:ABA52421.1,
RC ECO:0000313|Proteomes:UP000002700};
RA Woods D.E., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP000125; ABA52421.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3JJJ4; -.
DR SMR; Q3JJJ4; -.
DR MEROPS; S08.107; -.
DR EnsemblBacteria; ABA52421; ABA52421; BURPS1710b_A1101.
DR KEGG; bpm:BURPS1710b_A1101; -.
DR HOGENOM; CLU_011263_8_1_4; -.
DR Proteomes; UP000002700; Chromosome II.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07496; Peptidases_S8_13; 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; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034176; Peptidases_S8_13.
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; 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}; Metalloprotease {ECO:0000313|EMBL:ABA52421.1};
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}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004226785"
FT DOMAIN 191..471
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 223..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 437
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 500 AA; 50235 MW; 8B83247AB89611BF CRC64;
MSILIRTASF KATVLCAALA GLVSAAQAET AAAPQVPGPA DAVNQLIVKL RAVKTPPGAT
AAKAERADVQ AVIDRVLAAR NARAAGRAFG AAAASAPGNP DDPAAGIRIK RDMSGGATVL
SLQRHVSLAQ AEALARDFAA DGAIEYAEPD ARMHPFVVPN DTRYSEQWGY FNPTAGANLP
KAWDRTTGSA RVVVAVIDTG YRPHADLAAN LLPGYDFISD IPSANDGNGR DSDASDPGDW
VSAQEDGDPS GPFYGCGASD SSWHGTHVAG TIGAVTNNGV GVAGISWVGK VLPVRVLGKC
GGMLSDIADG MRWAAGLPVP GAPSNPNPAK VLNLSLGGYG RTCSSTYQNA INEITSRGAN
VVVAAGNNGG SVSTTQPANC RGVIAVGAID SRGVRASFSN TGAAVKISAP GVGILSTLNA
GKTSPGADSY ASYSGTSMAT PHVAGTVALM LAVNSTLSPS QILQRLQSSA RPFSSGSSCS
TSTCGAGLLD AGNAVDAAAQ
//
