ID F5XJE7_MICPN Unreviewed; 778 AA.
AC F5XJE7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=GTP pyrophosphokinase/guanosine-3',5'-bis (Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:BAK35847.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:BAK35847.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:BAK35847.1};
GN Name=relA {ECO:0000313|EMBL:BAK35847.1};
GN OrderedLocusNames=MLP_28330 {ECO:0000313|EMBL:BAK35847.1};
OS Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC
OS 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Microlunatus.
OX NCBI_TaxID=1032480 {ECO:0000313|EMBL:BAK35847.1, ECO:0000313|Proteomes:UP000007947};
RN [1] {ECO:0000313|EMBL:BAK35847.1, ECO:0000313|Proteomes:UP000007947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414
RC / VKM Ac-1990 / NM-1 {ECO:0000313|Proteomes:UP000007947};
RA Hosoyama A., Sasaki K., Harada T., Igarashi R., Kawakoshi A., Sasagawa M.,
RA Fukada J., Nakamura S., Katano Y., Hanada S., Kamagata Y., Nakamura N.,
RA Yamazaki S., Fujita N.;
RT "Whole genome sequence of Microlunatus phosphovorus NM-1.";
RL Submitted (MAY-2011) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; AP012204; BAK35847.1; -; Genomic_DNA.
DR AlphaFoldDB; F5XJE7; -.
DR STRING; 1032480.MLP_28330; -.
DR KEGG; mph:MLP_28330; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000007947; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000313|EMBL:BAK35847.1};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAK35847.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000007947};
KW Transferase {ECO:0000313|EMBL:BAK35847.1}.
FT DOMAIN 96..193
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 436..499
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 704..778
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 86964 MW; 1010CE489CD4AE2A CRC64;
MRPEPAETLS PGSPASAAPP PTPVVRVVPE SEQPRVRMRQ RIARFGAGKA QAPVLDPLFK
VIRANHPKAD LALIERAYRT AERYHRGQTR KSGDAFITHP LAVTTILAEL GMTETTLCAA
LLHDTVEDTA YTLEALTHDF GDKVALLVDG CTKLDKVKYG ESAKSETIRK MIIAMSRDIR
VLVIKLADRL HNMRTLHYLR PDKQYRIASE TLEIFAPLAH RLGMNAIKWE LEDLSFATMQ
PKVYDEIVRM VAEAAPRRDE FLSQVIEQVN ADLRAAKIRA TVTGRPKHYY SIYQKMVVRR
RDFADIFDLV GLRILVDSTR DCYAALGVMH VRWNPLPGRF KDYIAMPKFN MYQSLHTTVL
GPQGKPVELQ IRTEEMHKRA EFGVAAHWKY KEGGKALAET ATGSSDDLTW VRLLLDWQRE
TTDPGEFLDS LRFEINSSQV YTFTPNGDIH ALPQGATPVD FAYAIHTEVG HRTIGARVNG
RLVALESQLS NGDVVEILTT KSPDAGPKRD WLEFAKSPRA RNKIRHYFTR TRREESIENG
KEAIAKQLRK AGLPLQRLLT VEHLTAVADY FKLRDVPGLY AAVGEGTVGS QAVINRLIEA
EGGQDATADE INEDQVVTGR RRRKRSASDS GIEIDGDTDL LVKLAKCCTP VPGDDIIGFI
TRGAGVSVHR SDCVNADHLR TEHAERIIGV GWAPPTAQSS FLVAIQVEAL DRNRLLSDIT
RALSDQHVNI LSAALNTTKD KICKARFTFE TADPTHLDHV LRGVRQVPGV FDVYRIRQ
//
