ID A0A1Q9HH17_9VIBR Unreviewed; 739 AA.
AC A0A1Q9HH17;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:OLQ89274.1};
GN ORFNames=BIY22_20210 {ECO:0000313|EMBL:OLQ89274.1}, F7O85_01635
GN {ECO:0000313|EMBL:KAB1460082.1};
OS Vibrio panuliri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ89274.1, ECO:0000313|Proteomes:UP000186313};
RN [1] {ECO:0000313|EMBL:OLQ89274.1, ECO:0000313|Proteomes:UP000186313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ89274.1,
RC ECO:0000313|Proteomes:UP000186313};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAB1460082.1, ECO:0000313|Proteomes:UP000446972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBS 2 {ECO:0000313|EMBL:KAB1460082.1,
RC ECO:0000313|Proteomes:UP000446972};
RA Das S.S.;
RT "Whole genome sequence of Vibrio panuliri LBS 2.";
RL Submitted (SEP-2019) 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:OLQ89274.1}.
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DR EMBL; WAHU01000005; KAB1460082.1; -; Genomic_DNA.
DR EMBL; MJMJ01000016; OLQ89274.1; -; Genomic_DNA.
DR RefSeq; WP_075708912.1; NZ_WAHU01000005.1.
DR AlphaFoldDB; A0A1Q9HH17; -.
DR STRING; 1381081.BIY22_20210; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000186313; Unassembled WGS sequence.
DR Proteomes; UP000446972; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; 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: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; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:OLQ89274.1};
KW Transferase {ECO:0000313|EMBL:KAB1460082.1}.
FT DOMAIN 54..159
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 400..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 665..739
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 739 AA; 83964 MW; 41ECD0DCA179B280 CRC64;
MVAVRSAHLN QDEQFELDKW ITSLKQEPQT AQRLTQVYHQ CESYLQGNDN APLLLWRGRE
MIEILITLSM DKPTLIAALL FPLVSSGALQ REKLEEDFSK EIIKLIDGVE EMAALGQLNV
TLEGSAASAQ VDNVRRMLLA MVDDFRCVVI KLAERICNLI EVKKAPDEVR RAVAKECANI
YAPLANRLGI GQLKWEIEDY AFRYQQPDTY KQIAKQLSER RIVREQYIKD FVDDLLKEMK
VSAINADVSG RPKHIYSIWR KMQKKGLEFD ELFDVRAVRI IADKLQDCYA ALGVVHTKYK
HLPSEFDDYV ANPKPNGYQS IHTVILGPEG KTIEIQIRTK QMHEDSELGV AAHWKYKEGG
SGRSGYDEKI TWLRKLLDWQ EEMSDSGEML DEVRSQVFDD RVYAFTPRGD VVDLPMGATP
LDFAYHIHSM VGHRCIGAKV GGRIVPFTHK LQMGDQVEII TQKEPNPSRD WLNPSTGFVT
SGRARAKINA WFRKQSREKN LEAGREILEH ELAKIGATLK DAEQYALKRF NMNTSDELFV
GIGSGDLRIN QIINHINALV NKPTAEEEDQ QALEKLLEAE SKPSAPSRPN KDAVVVEGVD
NLMTHLARCC QPIPGDEIKG YITQGRGISV HRADCEQLEE LRHHAPERII DTVWGSGFAG
TYSLTLRVEA MERSGLLKEI TTLFANEKVK VNSMKSRVDY RNQLSILDFD LEVTTVEVVN
RLISRVEQIR DVMLVKRLG
//
