ID A0A0R0AK02_9GAMM Unreviewed; 716 AA.
AC A0A0R0AK02;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=(P)ppGpp synthetase {ECO:0000313|EMBL:KRG44809.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:KRG44809.1};
GN Name=relA {ECO:0000313|EMBL:KRG44809.1};
GN ORFNames=ARC20_07850 {ECO:0000313|EMBL:KRG44809.1};
OS Stenotrophomonas panacihumi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=676599 {ECO:0000313|EMBL:KRG44809.1, ECO:0000313|Proteomes:UP000051802};
RN [1] {ECO:0000313|EMBL:KRG44809.1, ECO:0000313|Proteomes:UP000051802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16536 {ECO:0000313|EMBL:KRG44809.1,
RC ECO:0000313|Proteomes:UP000051802};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (OCT-2015) 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 GDP: step
CC 1/1. {ECO:0000256|ARBA:ARBA00024329}.
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:KRG44809.1}.
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DR EMBL; LLXU01000066; KRG44809.1; -; Genomic_DNA.
DR RefSeq; WP_057646041.1; NZ_PZOY01000010.1.
DR AlphaFoldDB; A0A0R0AK02; -.
DR STRING; 676599.ARC20_07850; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000051802; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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; 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; 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:UP000051802};
KW Transferase {ECO:0000313|EMBL:KRG44809.1}.
FT DOMAIN 389..450
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 642..716
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 716 AA; 79470 MW; E9F2A7547D072F40 CRC64;
MHRPPPAHLQ DLLDRRSAAA IAPALREALL QAWSAQPAAA EAVPAWPVLA ETLDLLHLLS
ADEATLVAAL LFDLPALRGA VVELPLDAPR RQVLAGLLEG QDAADQVWAL HAGREAGRNS
EGLRRLLLAI IHDLRVVPIL LSRQLARMRA ASRLPEAGRR ALAQLTRDIH APLANRLGIW
QLKWELEDLA FRYLEPDTYR RIAREVDETR VERERYIESV RRALTHALAE HGLHAEVSGR
PKHIYSIWRK MQKKRLAFDQ LYDVRALRVM VDDVAACYAA LGVVHALWAP VPSEFDDYIA
RPKANDYRSL HTAVVGPEGR TVEVQIRTHE MHAQAELGVA AHWKYKEGGK GAEKAFDRKI
TWMRQLLEQS QEGEAGELAG ALDAELVEDR VYALTPKGEV IDLPQGATPL DFAYHVHTMV
GHRCRGAKVN GRIVPLAYKL RSGDRVEVLT AKEADPRRDW LLPANGFLAS GRSRDKVRAW
FHKLDRTRNV QAGRELLDRE LKRLGLQQAD LMIAAKRFHA DSVDDLYIQV ALGDTGPSQV
SRALLEAERA QQAPPPLPRP TAKRTGLGKS KFTVLGVGNL LVQLARCCQP VAGEPIVGYL
TQARGVTVHR ADCASLARLG AANPQRLLPV EWGQAGSGYE VDVQVRAVDR RYLLKDVTNL
IAQEDAHVLE INSDNVRDSG QAQLRLRLKV SDYGQLSTLL GKLDALPGVH QVRRLG
//
