ID S2VI41_9ACTO Unreviewed; 767 AA.
AC S2VI41;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EPD27118.1};
GN ORFNames=HMPREF9237_01061 {ECO:0000313|EMBL:EPD27118.1};
OS Actinotignum schaalii FB123-CNA-2.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=883067 {ECO:0000313|EMBL:EPD27118.1, ECO:0000313|Proteomes:UP000014393};
RN [1] {ECO:0000313|EMBL:EPD27118.1, ECO:0000313|Proteomes:UP000014393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB123-CNA-2 {ECO:0000313|EMBL:EPD27118.1,
RC ECO:0000313|Proteomes:UP000014393};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Saerens B., Vaneechoutte M.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Actinobaculum schaalii FB123-CNA2.";
RL Submitted (MAY-2013) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
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:EPD27118.1}.
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DR EMBL; AGWM01000010; EPD27118.1; -; Genomic_DNA.
DR RefSeq; WP_016442678.1; NZ_KE150262.1.
DR AlphaFoldDB; S2VI41; -.
DR STRING; 59505.FB03_01610; -.
DR PATRIC; fig|883067.3.peg.1035; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000014393; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000014393};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 65..162
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 412..473
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 679..753
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 767 AA; 86102 MW; 02F8293FA9BBF6D3 CRC64;
MSESQGPRVL SRLSWLTGRT ASQVPDALEP LMRALGNVDK ERIIRAYNVA EECHRGQKRR
SGEPYITHPV AVATILAELG MDEDTLVGAL LHDTVEDTGY TLEQVRDNFG STVELLVDGV
TKLDKVEYGE AAQAETVRKM VIAMSKDIRV LLIKLADRLH NARTWRFMPQ EKARSKAHET
LEIYAPLAHR LGMNSIKWEL EDLSFKTMYP EVYAEIESLV QERTPEREAY IAKIKAILER
ELKSSHIKCT ITGRPKHYYS IYQKMILRGK DFEDIYDLVG VRVLVETIPD CYAVLGVANT
IFTPIQGRIK DYITTPKFNL YQSIHTTVIG PDNRSLEIQI RTYDMHRRAE YGVAAHWRYK
ENPNATKRGG GTAKVDEETT QLNWLRQLVD WQRETADPAE FLESLSYEIS GNKVYVFTPA
GEVMELPTGA TPVDFAYAVH TEVGHRTVGA RVNDRLVTLD HKLESGDTVE IITAKSPDAG
PSLGWLDFVA SPRARAKIRV WFKKSRRDEA VEEGKDKLAR AIRKRNQPVQ RLMSHDTLAE
VAREAGRSSV DDLYAGIGEG DISPETVVRN LITSQGGQAG VEETLAEAVT PNRISRRRST
ASTDNAVVVQ GMEAGDVMVK LARCCTPVPP DSIVGFVTRG SGVSIHRADC PNVEQLQKQP
ERFLEVHWAD DSEAVYVIQV QVDALDRQGL LSDISRALLD NGVNLLAGNM MTTKERMVRN
TFTFEMADPH HLARVLADLR KIEGVYDAYR VTNSKPANQR RVESPRA
//
