ID Q2SUJ9_BURTA Unreviewed; 616 AA.
AC Q2SUJ9;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Peptidase, M24 family protein {ECO:0000313|EMBL:ABC38344.1};
GN OrderedLocusNames=BTH_I2888 {ECO:0000313|EMBL:ABC38344.1};
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:ABC38344.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC38344.1, 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 -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
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DR EMBL; CP000086; ABC38344.1; -; Genomic_DNA.
DR RefSeq; WP_009892110.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SUJ9; -.
DR KEGG; bte:BTH_I2888; -.
DR HOGENOM; CLU_430044_0_0_4; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 26..148
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 346..559
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 616 AA; 67524 MW; 972F5E25C70DE18A CRC64;
MIDRLKYSFT DLARYDASVV DTHAGLSHLI DALQLDALVV TSQDEYISEW LPRCNNPRYA
LSGFDGSVGS GVFLSAAAAK RIGVPQFVLF VDGRYHLQAE KQCDPVRVHV EKLGLNVAMW
PAIGDWLATH AADIKRVGYD APRLSVAQRA CLFAQTRSAG LQWTSLADSE IDQAISLPGW
RVERPIFELP RSVTGVSIAE NVATLNKRIG EHLGDPCAKA AFLSCAADDL SYLLNSRGYH
LPYVSSHVGF LFVVGDAVAL FLPEGFDRCP VQVDSYPALH VIRNDAAALE RFLAQFDIEY
VCYGFEAVNC ALPDAVRRVW PVARHVDHNP VEAMRAAKTP EVLGQFRDAF ARSSDAIAEA
MRWAKKGEPG KRHSEFDLAR VISDAYAARS AVALSFTTVA ANGANSASAH YTAVSPDVEL
TEGELVLLDS GAYFDGGFAT DCTRVVLRRT RADTQPQPWQ REIYTVALKA CIKGLVTRFP
QTATGADVDA VVRGVCREHG YDYNHGTGHG IGIHVHEGGV RFNVGSQYGL VPNAVISVEP
GIYLPGKGGV RIENIVVIHP SEREPGKMEF ENLVTVGYDW DLIDVDLLTD DERAYLRDYE
RLCVERGTNV TDCPLL
//
