ID   A0A061AJ38_9MOLU        Unreviewed;       723 AA.
AC   A0A061AJ38;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:CDR31007.1};
GN   Name=relA {ECO:0000313|EMBL:CDR31007.1};
GN   ORFNames=Aocu_09340 {ECO:0000313|EMBL:CDR31007.1};
OS   Acholeplasma oculi.
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=35623 {ECO:0000313|EMBL:CDR31007.1, ECO:0000313|Proteomes:UP000032434};
RN   [1] {ECO:0000313|Proteomes:UP000032434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kube M.;
RL   Submitted (MAY-2014) 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}.
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DR   EMBL; LK028559; CDR31007.1; -; Genomic_DNA.
DR   RefSeq; WP_045749473.1; NZ_UFRU01000001.1.
DR   AlphaFoldDB; A0A061AJ38; -.
DR   STRING; 35623.Aocu_09340; -.
DR   KEGG; aoc:Aocu_09340; -.
DR   PATRIC; fig|35623.3.peg.933; -.
DR   HOGENOM; CLU_012300_3_0_14; -.
DR   InParanoid; A0A061AJ38; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000032434; Chromosome.
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; 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; 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; IPR045600; RelA/SpoT_AH_RIS.
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; PF19296; RelA_AH_RIS; 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; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81271; TGS-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:CDR31007.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032434};
KW   Transferase {ECO:0000313|EMBL:CDR31007.1}.
FT   DOMAIN          48..145
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          394..457
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
SQ   SEQUENCE   723 AA;  82091 MW;  8035122088DB1AC1 CRC64;
     MNDALYKALM SDISHYIKSE TNIKLITKAY ELAKQKHLGQ MRKSGEPYIT HPVAVARILS
     ELEAGPITLV GALLHDTVED TDYTLKELEQ DFGKDAALLV DGVTKLSKIS FQNTEQSDNQ
     QKMLIAMAKD IRVVLIKIAD RLHNMRTLNS MSSEKQVSIS KETLDIYAPI AHRLGLFRWK
     AELEDRSLRF VDPAMYYKVS NLVKAKRTER ENNIENVIEY IKTLFEESEL KNFEIKGRIK
     NIYSIYKKMV NGGRSFEDIY DLLAVRVIVD KVETCYQSLG IIHAHFTPIP KRFKDYIAVP
     KPNLYQSLHT TVLHSDGTLF EVQIRTKEMD KVAEDGIAAH WAYKENKVYS KEREQFEIAS
     KLKWYAELLK IAEDKDDQAG TSQEFVDTVK TDIFSANVYV FTPKGEVIEL PHGSTPIDFA
     YRIHTDVGHK MVGAIVNGRI VTLDHELQTG DVVSIKTNKN SSGPSEDWLK IAQSPHARHK
     IKGFINKGNQ EITLSTGKEL LEKELILNKR DDILDDEWVE KNFEKSGIET LNELYLEIGK
     GNISTKTVMN RLIPEITKEM LIQRQIERTQ RQLIAISETG VVIEGLSNPQ IKLANCCTPI
     PGDEISGYVT KGSGIVVHAN HCTNLKQYDS KRLITALWGT NLTRKYATWL KIKGTSRTGL
     LTDIIQVANA NGIAIAEVSA VTNQEFESII RLKVTLNKRS ELDTLMVNIQ KVPQVYYVER
     DMQ
//