ID K9WPE6_9CYAN Unreviewed; 751 AA.
AC K9WPE6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=(P)ppGpp synthetase, RelA/SpoT family {ECO:0000313|EMBL:AFZ21422.1};
GN ORFNames=Mic7113_5802 {ECO:0000313|EMBL:AFZ21422.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ21422.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ21422.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ21422.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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 -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP003630; AFZ21422.1; -; Genomic_DNA.
DR RefSeq; WP_015185551.1; NC_019738.1.
DR AlphaFoldDB; K9WPE6; -.
DR STRING; 1173027.Mic7113_5802; -.
DR KEGG; mic:Mic7113_5802; -.
DR PATRIC; fig|1173027.3.peg.6423; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_3; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000010471; Chromosome.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 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; IPR003607; HD/PDEase_dom.
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: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; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 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 Reference proteome {ECO:0000313|Proteomes:UP000010471}.
FT DOMAIN 62..161
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 407..468
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 672..746
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 570..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 751 AA; 85115 MW; 8137FF7BF6723172 CRC64;
MDAIATTSRF NFDVPEWLQE CILATSAAAN EPVPDDINLI SRAFEFAYKL HEGQLRASGE
PYIAHPVAVA GLLRDLGGSS VMIAAGFLHD VVEDTDVTPE EIESRFGVEV RRLVEGVTKL
SKFNFSSKTE RQAENFRRMF LAMAADIRVI VVKLADRLHN MRTLEHLNPQ KQRSISQETR
EIFAPLANRL GIGRVKWELE DLAFKYLEPE SYRQMQQLVA ERRTDRETRL SKVGDILRER
LESTEIHCLE ISGRPKHLYG IYQKMQRQQK GFHEIYDLAA MRLILQTKED CYRALAIVHD
AFRPIPGRFK DYIGLPKPNR YQSLHTGVMG PSGRPIEVQI RTLEMHHIAE YGIAAHWKYK
ESGGSSNNRI SAEDEKFTWL RQLLEWQNDL KDAQEYMDTI KDNLFDDDVY VFTPNGDVIP
LSRGATPVDF AYRIHSEVGN HCAGARVNGR WTVLDTPLNN GDIVEIITKE NSHPSLDWLN
FVATPSARNR IRQWYKRSHR DANVARGKEL LEKELGKRGF EALLKSEPMQ AAAERCNYHS
VEDLLAALGY GELTLNLVVK RLREAVKARQ PLETEPQEPL IPQPPVAKPQ ATGGAKKIEP
IAGVEGLLHH LAGCCNPIPG EAIIGVVTRT RGISIHRQGC LNVESVPGER VIPVSWNPTD
VAHGRPQTYP VNIQIEVIDR VGVFKDILSR LSDQNINVRN AQVRTQEGRP AIIDLCIDIC
DHQQLERSFC QIKKMSDILN IRRVSQVEEA C
//
