ID A0A031LWA4_9GAMM Unreviewed; 768 AA.
AC A0A031LWA4;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=GTP pyrophosphokinase {ECO:0000256|ARBA:ARBA00019852};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
DE AltName: Full=(p)ppGpp synthase {ECO:0000256|ARBA:ARBA00032407};
DE AltName: Full=ATP:GTP 3'-pyrophosphotransferase {ECO:0000256|ARBA:ARBA00029754};
DE AltName: Full=ppGpp synthase I {ECO:0000256|ARBA:ARBA00033308};
GN ORFNames=CL42_03760 {ECO:0000313|EMBL:EZQ11784.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ11784.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ11784.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ11784.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-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 -!- 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}.
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:EZQ11784.1}.
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DR EMBL; JFYL01000007; EZQ11784.1; -; Genomic_DNA.
DR RefSeq; WP_035265331.1; NZ_JFYL01000007.1.
DR AlphaFoldDB; A0A031LWA4; -.
DR eggNOG; COG0317; Bacteria.
DR Proteomes; UP000023816; 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; 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; 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:SF40; GTP PYROPHOSPHOKINASE; 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; 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; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:EZQ11784.1};
KW Transferase {ECO:0000313|EMBL:EZQ11784.1}.
FT DOMAIN 430..493
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 692..766
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 768 AA; 88117 MW; EAAE3FEC1B21D39C CRC64;
MVTVREQLPG RLTELSEETT VEHAAEAQLG LATWLDRARI ILDGAELKKL EEVALSVLKK
ELTSDHHHKT NTFATGLGMA DILAHLHVDE DTLSAAMLYR SVREGMTSLE EIRKSFGESV
YNLVKGTLAM GKLSELIEKN KRLEDHFNNN QREHLTGIYK MLISVTEDVR VVLIKLAERT
LALRELANSP KERQERVARE ILTIYSPLAH RLGIAQLKWE LEDLAFRYLA PERYKEIASL
LNEKRLEREQ YIQFVVDKLK SELLKHGIEA EISGRVKHIY SIYRKMKSKN LSFDQLYDIR
AVRVLVQNVS ECYHALGIVH QIWRHIPHQF DDYITNPKAN GYRSLHTAVI AENKSLEIQI
RTTEMHEEAE LGVCSHFNYK EGAKTTDYSF NHRLHSLRSV LEHYQERNEA GAHPNEDETE
NFNQLQDFED FEKIYVFSRD GDIKELPRNS TVLDFAYHVH TEVGNKCYAA RVNQRYVPLT
YTLKTGEQVE ILTKKDREPN RDWLVNSLGY IKTARARDKL RHWFRQQDRS KNLEVGREIL
TKELSRLAIH PKSIDLSDYC AHFNVKTGED ILVSLVSGDI SLHALINQVN RHMHLDQDEP
ELVLKPALNP RASHTLSAHG ILIDGLDNVE LHIAQCCQPV HGESIAGYIT LNRGVSIHKV
ACPDYVRMIS QEPERAVEAD WEMQPTRGQS VQIVVEAYDR RGLLKDLTQV IFSDQINIRQ
VNTISEADGI ANMKLLIEVK GLAQLSRLLA RLEQQPGIIS ARRLVQGN
//