ID M3FF34_LEPBO Unreviewed; 674 AA.
AC M3FF34;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative GTP diphosphokinase {ECO:0000313|EMBL:EMG00473.1};
GN ORFNames=LEP1GSC123_4052 {ECO:0000313|EMBL:EMG00473.1};
OS Leptospira borgpetersenii str. 200701203.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193007 {ECO:0000313|EMBL:EMG00473.1, ECO:0000313|Proteomes:UP000011783};
RN [1] {ECO:0000313|EMBL:EMG00473.1, ECO:0000313|Proteomes:UP000011783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200701203 {ECO:0000313|EMBL:EMG00473.1,
RC ECO:0000313|Proteomes:UP000011783};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EMG00473.1}.
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DR EMBL; AKWO02000046; EMG00473.1; -; Genomic_DNA.
DR AlphaFoldDB; M3FF34; -.
DR BioCyc; LBOR1193007:G11KN-3921-MONOMER; -.
DR Proteomes; UP000011783; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 Kinase {ECO:0000313|EMBL:EMG00473.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011783};
KW Transferase {ECO:0000313|EMBL:EMG00473.1}.
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; 76725 MW; 0E12BFCBCCA98D3F CRC64;
MGFVKTPATK DMLLEGVRET LGESAYESVQ KAYDVSERAH QGQFRLSGEP YIVHPLQVGF
ILYELGLDEK VICAGLLHDV IEDTQYSRDD MIRDFGEDIT DLVEGVTKIS KIKSQSKETE
AAENIRKIIV ATIKDIRVIL IKLADKTHNM RTLSFQLPEK QKRIAQETLS LYAPIAGRLG
IYKIKSELED LAFQVLNPEE YQEVKKNINS KKSEREGFIE TLKIILLQRL SEIQIEADVD
GRAKHFYSIY RKMKLKEKTF NEIFDLRAIR IITNEVKDCY GVLGIVHTLW NPVPGRFKDY
IATPKTNMYQ SLHTTVIGPD GKPLEVQIRT RDMNDIAEYG IAAHWMYKEG KPSLSEKNVK
VRWLELLSSW QDSALDPKEF VEELKYDLHE DEVFVFTPKG EILQLPKGAT ILDFAFRIHT
DVGLKAKGGR INGRMLPLRT ELRSGDQIEI ITDKRTKPSP IWLRIVRTPS ARQKLRSYFR
KLKEENKKDL QQEAEFAAEI TLNVEVLEEL KKKPLAKPAK QIDLGAGKVI VAGLRGIPAR
LSGCCSPLPG DGIIGFVTRG RGVSIHKKGC ATAKQQEQEE SMRIITVEWD YGQSESIPVL
IEVKSKDRQG IFMEIVKSIS NTQTNIRESK ASTDQRGNLV ANFEVDVEHL DQLKEILSNL
KQIPDVYQAH RIKN
//
