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Database: UniProt
Entry: Q72TK7_LEPIC
LinkDB: Q72TK7_LEPIC
Original site: Q72TK7_LEPIC 
ID   Q72TK7_LEPIC            Unreviewed;       674 AA.
AC   Q72TK7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=Guanosine polyphosphate pyrophosphohydrolases/synthetases {ECO:0000313|EMBL:AAS69621.1};
GN   OrderedLocusNames=LIC_11012 {ECO:0000313|EMBL:AAS69621.1};
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=267671 {ECO:0000313|EMBL:AAS69621.1, ECO:0000313|Proteomes:UP000007037};
RN   [1] {ECO:0000313|EMBL:AAS69621.1, ECO:0000313|Proteomes:UP000007037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130 {ECO:0000313|EMBL:AAS69621.1,
RC   ECO:0000313|Proteomes:UP000007037};
RX   PubMed=15028702; DOI=10.1128/JB.186.7.2164-2172.2004;
RA   Nascimento A.L., Ko A.I., Martins E.A., Monteiro-Vitorello C.B., Ho P.L.,
RA   Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F., Leite L.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H., Harakava R., Jeronimo S.M., Junqueira-De-Azevedo I.L.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G., Lemos M.V., Marino C.L., Nunes L.R.,
RA   De Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J.,
RA   Sommer P., Tsai S.M., Simpson A.J., Ferro J.A., Camargo L.E.,
RA   Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
CC   -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC       is a mediator of the stringent response that coordinates a variety of
CC       cellular activities in response to changes in nutritional abundance.
CC       {ECO:0000256|RuleBase:RU003847}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; AE016823; AAS69621.1; -; Genomic_DNA.
DR   RefSeq; WP_000508128.1; NC_005823.1.
DR   AlphaFoldDB; Q72TK7; -.
DR   GeneID; 61144336; -.
DR   KEGG; lic:LIC_11012; -.
DR   HOGENOM; CLU_012300_3_0_12; -.
DR   Proteomes; UP000007037; Chromosome I.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR   CDD; cd04876; ACT_RelA-SpoT; 1.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05399; NT_Rel-Spo_like; 1.
DR   CDD; cd01668; TGS_RSH; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR004811; RelA/Spo_fam.
DR   InterPro; IPR007685; RelA_SpoT.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   InterPro; IPR033655; TGS_RelA/SpoT.
DR   NCBIfam; TIGR00691; spoT_relA; 1.
DR   PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR   PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR   Pfam; PF13291; ACT_4; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   Pfam; PF04607; RelA_SpoT; 1.
DR   Pfam; PF02824; TGS; 1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00954; RelA_SpoT; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AAS69621.1}.
FT   DOMAIN          51..150
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          391..452
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          600..674
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   674 AA;  76670 MW;  9E544FAC3FF534E3 CRC64;
     MGFVKAPVTK DILLEGVCQK LGDHAYESVQ KAYDVSERAH QGQFRLSGEP YIVHPLQVGF
     ILYELGLDEK VICAGLLHDV IEDTEYSRED MIRDFGEDIT DLVEGVTKIS KIKSQSKETE
     AAENIRKIIV ATIKDIRVIL IKLADKTHNL RTLSFQPPEK QRRIAQETLS LYAPIAGRLG
     IYKIKSELED LAFQILNPDE YQEVKKNINS KKSEREGFIE TLKIILLQRL SEIQIEADVD
     GRAKHFYSIY RKMKLKEKTF NEIFDLRAIR IITNEVKDCY GVLGIVHTLW NPVPGRFKDY
     IATPKTNMYQ SLHTTVIGPD GKPLEVQIRT RDMNDIAEYG IAAHWIYKEG KPSASEKNVK
     VKWLELLSSW QDSALDPKEF VEELKYDLHE DEVFVFTPKG EILQLPKGAT ILDFAFRIHT
     DVGLKAKGGR INGRMLPLRT ELRSGDQIEI ITDKRTKPSP IWLRIVRTPS ARQKLRSYFK
     KLREENKKDL QQEAEFAAEI TLNVDVLEEL KKKPSSKPTK QIDLAAGKVI VAGLRGIPVR
     LSGCCSPLPG DGIIGFVTRG RGVSIHKKGC VTAKQQEQEE SMRVITVEWD YGQSESIPVL
     IEVKSKDRQG IFMEIVKSIS NTQTNIRESK ASTDQRGNLV ASFEVDVEHL DQLKEILSNL
     KQIPDVYQAH RIKN
//
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