ID C5AG42_BURGB Unreviewed; 509 AA.
AC C5AG42;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Serine metalloprotease {ECO:0000313|EMBL:ACR28799.1};
GN OrderedLocusNames=bglu_1g16590 {ECO:0000313|EMBL:ACR28799.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR28799.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR28799.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR28799.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(2009).
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; CP001503; ACR28799.1; -; Genomic_DNA.
DR RefSeq; WP_015875691.1; NC_012724.2.
DR AlphaFoldDB; C5AG42; -.
DR STRING; 626418.bglu_1g16590; -.
DR MEROPS; S08.107; -.
DR KEGG; bgl:bglu_1g16590; -.
DR PATRIC; fig|626418.3.peg.4451; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_8_1_4; -.
DR PHI-base; PHI:8850; -.
DR Proteomes; UP000002187; Chromosome 1.
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:ACR28799.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000002187};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..509
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002947650"
FT DOMAIN 192..480
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 222..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 274
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 446
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 509 AA; 51234 MW; 1651D6BB76D158DB CRC64;
MKKSVRTTSH LKLASFLLAA CASFAQAQTP SPSTPATGAA SENINQLIVK LKPAAAAARG
STSITTAAAD IHGVIDRVLA ARRARATTRA FGAAAASAPG NAGDPAANIS VKREMADGAT
VLRLQRSLPA ADAAALANDF AADAAVEYAE PDAHMHALLV PNDTRYGEQW GYASGIGGAN
LPKAWDITTG SANVVVAVVD TGYRPHSDLA ANVLPGYDFI SDPNSANDGN GRDSDATDPG
DWVSQSEVDD PDGPFYRCQV DQYGRTFASD SSWHGTHVAG TIGAVSNNGR GVAGISWKGK
ILPVRVLGKC GGALSDIADG MRWAAGLSVP GVPANRTPAR VLNFSLGGGG SCSRTYQSAI
NAVVAAGATV VVAAGNEAAQ VSTSQPANCQ NVIAVAATDV NGRRASFSNY GSAVKIAAPG
VNILSTLNSG KTSPAADSYA SYNGTSMATP HVAGTVALML AANGSLTPAQ VLQKLQASAR
PFPSGSGCST STCGAGLLDA GAAVSAARQ
//
