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Database: UniProt
Entry: E1QH57_DESB2
LinkDB: E1QH57_DESB2
Original site: E1QH57_DESB2 
ID   E1QH57_DESB2            Unreviewed;       460 AA.
AC   E1QH57;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Peptidase U62 modulator of DNA gyrase {ECO:0000313|EMBL:ADK84900.1};
GN   OrderedLocusNames=Deba_1532 {ECO:0000313|EMBL:ADK84900.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84900.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK84900.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
CC   -!- SIMILARITY: Belongs to the peptidase U62 family.
CC       {ECO:0000256|ARBA:ARBA00005836}.
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DR   EMBL; CP002085; ADK84900.1; -; Genomic_DNA.
DR   RefSeq; WP_013258353.1; NC_014365.1.
DR   AlphaFoldDB; E1QH57; -.
DR   STRING; 644282.Deba_1532; -.
DR   KEGG; dbr:Deba_1532; -.
DR   eggNOG; COG0312; Bacteria.
DR   HOGENOM; CLU_026425_1_0_7; -.
DR   OrthoDB; 9803618at2; -.
DR   Proteomes; UP000009047; Chromosome.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2290.10; PmbA/TldD superfamily; 1.
DR   InterPro; IPR045569; Metalloprtase-TldD/E_C.
DR   InterPro; IPR045570; Metalloprtase-TldD/E_cen_dom.
DR   InterPro; IPR002510; Metalloprtase-TldD/E_N.
DR   InterPro; IPR025502; TldD.
DR   InterPro; IPR035068; TldD/PmbA_N.
DR   InterPro; IPR036059; TldD/PmbA_sf.
DR   PANTHER; PTHR30624:SF4; METALLOPROTEASE TLDD; 1.
DR   PANTHER; PTHR30624; UNCHARACTERIZED PROTEIN TLDD AND PMBA; 1.
DR   Pfam; PF01523; PmbA_TldD_1st; 1.
DR   Pfam; PF19290; PmbA_TldD_2nd; 1.
DR   Pfam; PF19289; PmbA_TldD_3rd; 1.
DR   PIRSF; PIRSF004919; TldD; 1.
DR   SUPFAM; SSF111283; Putative modulator of DNA gyrase, PmbA/TldD; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009047}.
FT   DOMAIN          22..80
FT                   /note="Metalloprotease TldD/E N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01523"
FT   DOMAIN          110..218
FT                   /note="Metalloprotease TldD/E central"
FT                   /evidence="ECO:0000259|Pfam:PF19290"
FT   DOMAIN          226..457
FT                   /note="Metalloprotease TldD/E C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19289"
SQ   SEQUENCE   460 AA;  48203 MW;  97F4F02E6100A09F CRC64;
     MSLELDVTPA LEAALGGGGE MAEAFLEDSS SLMVVIDNAK VEKVLGGQDL GVGLRLIKDL
     RTSYAFGNQL RAQALVALAS DIAAERDAAP GRLHSFAPIA PGLAPAIVKP PIGVETARKV
     EMARTAEAAA RAVDNRVRQV RVIYLERTQR VRVVNSLGVD ARDERTQVLM AIHCVAAEGA
     VLQTGYESIG GLCGLELFDD QPPEQAARRA ARQAVMMLAA QPAPGGSMAV VLHSAAGGTM
     IHEAVGHGLE ADIVLEGMSV YKDQVGRQVA SPLITVIDDG SLAGKRGSAG FDDEGVPTGR
     NVLIAGGVLK GYLHDRLSAM KMNARPTGNG RRENYRQRPI PRMTNTFIAP GHDDPEAIIA
     DTPHGLLVKK MGGGQVNTTN GDFVFEVAEG YLIENGRVGR PVRGATLTGN GPKVLMDIDR
     VANDLGFGIG TCGKEGQGSP VADAQPTLRI PSIVVGGRQG
//
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