ID Q2T454_BURTA Unreviewed; 567 AA.
AC Q2T454;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Metallopeptidase domain protein {ECO:0000313|EMBL:ABC34146.1};
GN OrderedLocusNames=BTH_II1851 {ECO:0000313|EMBL:ABC34146.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC34146.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC34146.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000085; ABC34146.1; -; Genomic_DNA.
DR RefSeq; WP_009898026.1; NZ_CP008786.1.
DR AlphaFoldDB; Q2T454; -.
DR MEROPS; M04.026; -.
DR KEGG; bte:BTH_II1851; -.
DR HOGENOM; CLU_040771_0_0_4; -.
DR Proteomes; UP000001930; Chromosome II.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.170.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR001842; Peptidase_M36.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF3; NEUTRAL PROTEASE B; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..567
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007701220"
FT DOMAIN 107..146
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT REGION 27..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 567 AA; 60399 MW; 5541901E83A32F31 CRC64;
MQTSRKALPL ALSLAIGLGA ALPAWADSKA PNPQEESRRA SLTRGVVPPS EKADKTGQFR
PGTVAVTLAS PAFHAKKADA AAMAREFITA RATQLGLDKA ALANLVVASE RADATFTVVR
FQQRAAGLPV YDSDIAITVA PDGRVLYVAS KAVNGVAAVS SKTQAVDEQQ ALDRARAYLG
VSGFASVQSQ LVAFVDGTGT HTAWKVRGRP QDSLRGDWEL IIDANSGEVL RAEDKASYAT
DGTGLVFRPD PLSPTKSSYG STGFKDNNDA DSPQLSAARV RVTLKDLTQT SGGYKLAGPY
ASCVDFDAPF DKACPVQPSP TFDFTRSNLY FEAVNAYYHI DTFLRYVNLT LGIKALPYQY
SGGVQYDPHG ESGDDNSSYS SGSGRLSFGQ GGVDDAEDAD VVIHELGHGI HDWITNGGLS
QVEGLSEGTG DYLAAAYSRD FNQWSPSDAQ YHWVYNWDGH NEFWPGRVTN YNVGRTYAQV
RNSEIHTAGQ YWASCNMVAR DAIGGAAMDK AFLKGLSMTN GSTNQKAAAQ AVLTAAAALG
YSSAQLNAIG NAYNKSCTYG VTVPQKL
//
