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Database: UniProt
Entry: F3QR57_9BACT
LinkDB: F3QR57_9BACT
Original site: F3QR57_9BACT 
ID   F3QR57_9BACT            Unreviewed;       737 AA.
AC   F3QR57;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EGG56311.1};
GN   ORFNames=HMPREF9442_00656 {ECO:0000313|EMBL:EGG56311.1};
OS   Paraprevotella xylaniphila YIT 11841.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Paraprevotella.
OX   NCBI_TaxID=762982 {ECO:0000313|EMBL:EGG56311.1, ECO:0000313|Proteomes:UP000005546};
RN   [1] {ECO:0000313|EMBL:EGG56311.1, ECO:0000313|Proteomes:UP000005546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11841 {ECO:0000313|EMBL:EGG56311.1,
RC   ECO:0000313|Proteomes:UP000005546};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) 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}.
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:EGG56311.1}.
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DR   EMBL; AFBR01000020; EGG56311.1; -; Genomic_DNA.
DR   RefSeq; WP_008625157.1; NZ_LR215980.1.
DR   AlphaFoldDB; F3QR57; -.
DR   STRING; 762982.HMPREF9442_00656; -.
DR   eggNOG; COG0317; Bacteria.
DR   HOGENOM; CLU_012300_3_2_10; -.
DR   OrthoDB; 9805041at2; -.
DR   Proteomes; UP000005546; Unassembled WGS sequence.
DR   GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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: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; 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;
FT   DOMAIN          402..463
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          665..737
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   737 AA;  84373 MW;  73DD9FB66345A983 CRC64;
     MEQNAFFSAQ EKVRLAQLYR ELLKLSGNIL YPDDCKKLKT YLLEAVRRNL IQRNVFGMNP
     ILNDMETALI VASEIGLTRG AILGIMVHTC VRCGYCTTED VEREFGVDVA GIIKGLNRIL
     ELYDKNPSVE SENFRSLLLS FAEDMRVVLI MIANRVNIMR KIKDTENKEA QRKVSEEAAY
     LYAPLAHKLG LYRLKSELED LSLKYLEHDA YYLIKEKLNA TKKSRDEYIE KFIRPIDEKL
     KKAGLRFHMK GRTKSIHSIW QKMKKQHCGV EGIYDLFAIR IILDSALEKE KMECWQVYSI
     ITDMYQPNPK RLRDWLSIPK SNGYESLHIT VLGPENKWVE VQIRTERMDE IAERGLAAHW
     RYKGIKSGES GVDEWLNNIR SALENNDDLQ LMDQFKMDLY EDEVFVFTPK GDLFKFPKGA
     TVLDFAYAIH TNVGDHCIGA KINEKNAPLR QKLNSGDQVE ILTANNQSPK QDWLNFVVTG
     KARAKIRQAL KEMQAKQGAF AKELLERKFK NRKIEYDEPT MMHVIKKLGF KVVTDFYKSL
     ANETTDINEV LDLYTEQQKI EAGLAEHTPA PSAESYNIPS EAELKAKTND DVLVIDQNLK
     GLDFSLAKCC QPIYGDDVFG FVTVNGGIKI HRQDCPNAQE LRKRFGYRIV KARWAGKRGS
     QYPITLKVIG NDDLGIVNNI TSIISKEEKI SLRSISIDSH DGLFSGTLTV MLDDTSKLQL
     LEKKLKTIKG VKQVSRN
//
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