ID I4ZT13_9GAMM Unreviewed; 769 AA.
AC I4ZT13;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=HADU_07565 {ECO:0000313|EMBL:EIM39355.1};
OS Acinetobacter sp. HA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1173062 {ECO:0000313|EMBL:EIM39355.1, ECO:0000313|Proteomes:UP000018434};
RN [1] {ECO:0000313|EMBL:EIM39355.1, ECO:0000313|Proteomes:UP000018434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA {ECO:0000313|EMBL:EIM39355.1,
RC ECO:0000313|Proteomes:UP000018434};
RX PubMed=22933775; DOI=10.1128/JB.01194-12;
RA Malhotra J., Dua A., Saxena A., Sangwan N., Mukherjee U., Pandey N.,
RA Rajagopal R., Khurana P., Khurana J.P., Lal R.;
RT "Genome Sequence of Acinetobacter sp. Strain HA, Isolated from the Gut of
RT the Polyphagous Insect Pest Helicoverpa armigera.";
RL J. Bacteriol. 194:5156-5156(2012).
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:EIM39355.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJXD01000031; EIM39355.1; -; Genomic_DNA.
DR RefSeq; WP_005223232.1; NZ_AJXD01000031.1.
DR AlphaFoldDB; I4ZT13; -.
DR GeneID; 58162206; -.
DR PATRIC; fig|1173062.3.peg.1484; -.
DR Proteomes; UP000018434; Unassembled WGS sequence.
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; 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 Hydrolase {ECO:0000313|EMBL:EIM39355.1}.
FT DOMAIN 431..494
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 693..767
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 769 AA; 88266 MW; C194641C4194410B CRC64;
MVTVREQLPG RLNELSQEAT VEHADQALQD MTEWLDRVRG ILDGAPLKQL EEVAHLTLEN
ELETTVQHRS NTFYTGIEMA DILAHLHVDE DTLSAAMLYR SVREGVTPLA DVLEKFGESV
HGLVKGTLSM GKLSELIENN KRLEDHFNNN QREHLTGIYK MLISVTEDVR VVLIKLAERT
YALRELAKSP RDRQERVARE ILTIYSPLAH RLGIAQLKWE LEDLAFRYLA PERYKEIASL
LNEKRLEREH YIQFVIDKLR GELAEHGIEA EITGRVKHIY SIYRKMKSKD LSFDQLYDIR
AVRVLVNSVP ECYHTLGIVH QIWRHIPHQF DDYITNPKAN GYRSLHTAVI AENKSLEVQI
RTYHMHEEAE LGVCSHFNYK EGAKTTDHSF NHRLHSLRAV LEHYQERNDA SAHKDSEAEV
ENFEQIQDFE GFEKIYVFSR DGDIKELPRG STVLDFAYHV HTEVGNKCYA ARVNQRYVPL
TYTLKTGEQV EILTKKDREP NRDWLVNSLG YIKTARARDK LRHWFRQQDR SKNLEVGREI
LNKELSRLAI HPKSIDLGDY CNHFNVKSGE DILIGIVNGD ISLHALINQV NRHMHLDQDE
PELVLKPALN PRASHTLSAH GILIDGLDNV ELHVAQCCQP VHGESIGGYI TLNRGVSIHK
VACPDYVRMI SQEPERAVEA DWEMQPTRGQ SVQIVVEAYD RRGLLKDLTQ VIFSDQINIR
QVNTISEADG IANMKLLIEV KGLAQLSKLL ARLEQQPGII SARRLVQGN
//
