ID Q9CJX4_PASMU Unreviewed; 739 AA.
AC Q9CJX4;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 127.
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 Name=relA {ECO:0000313|EMBL:AAK03949.1};
GN OrderedLocusNames=PM1865 {ECO:0000313|EMBL:AAK03949.1};
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK03949.1, ECO:0000313|Proteomes:UP000000809};
RN [1] {ECO:0000313|EMBL:AAK03949.1, ECO:0000313|Proteomes:UP000000809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK03949.1,
RC ECO:0000313|Proteomes:UP000000809};
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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 ---------------------------------------------------------------------------
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; AE004439; AAK03949.1; -; Genomic_DNA.
DR RefSeq; WP_010907387.1; NC_002663.1.
DR AlphaFoldDB; Q9CJX4; -.
DR STRING; 272843.PM1865; -.
DR EnsemblBacteria; AAK03949; AAK03949; PM1865.
DR KEGG; pmu:PM1865; -.
DR PATRIC; fig|272843.6.peg.1887; -.
DR HOGENOM; CLU_012300_3_0_6; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000000809; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000000809}.
FT DOMAIN 401..462
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 666..739
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 739 AA; 84238 MW; 3740ED4043159AC2 CRC64;
MVAVRGSHLL NPKDFVIETW CASLEVSPEV RENLVNAWYY SQKYIPQHHD ASSCSLHSGV
EMVEILHSLN MDADSLLTAM LYPTIHHKLV ELSQINEDFG ANIYKLAKGV MEMDNIRQLN
ASQSANNAQV DNIRRMLLAM VDDFRCVIIK LAERITFLRD AEQTCSEEDK VLAAKECANI
YAPLANRLGI GQLKWELEDY CFRYLHPEQY RSIANLLKER RLDREQYIAD FVSEVSDYLR
HNIDKVDVYG RPKHIYSIWR KMQKKHLEFS DLYDVRAVRI IVPKLQDCYT ALGIVHTHFK
HIPKEFDDYV ANPKPNGYQS IHTVVLGKGG KPVEVQIRTQ QMHDDAELGV AAHWKYKEGA
TGGRSGYEEK ITWLRKLLAW QDDITDSGEI MAEMRSQVFD DRVYVFTPKG EVIDLPTGST
PLDFAYAIHS EIGHRCIGAK VSGRIVPFTY QLQMGDQIDI ITQKNANPSR DWLNPNLGFT
HTAKARAKIH AWFKKQDREK NIPAGKEMLE NELTRLNIGL KQIEPHALAR YNLKNLEDLY
AGIGGGDIRL NHLINFLQNK LIKTTAQEVD EEILRHVANK SAANNQQKEK PRGYVIVEGV
GNLMHHIARC CQPIPGDHIM GYITMGRGIS IHRSDCEQFL ELQQAHPERV VESIWGDNYA
SGFKISIRII ASDRSGLLRD ITTVLANDKI SVLGVSSRTD TKKQLATIDM EIELNNVQIL
SKILARLSKL DDVIEAKRL
//
