ID L1MMV3_9BACT Unreviewed; 749 AA.
AC L1MMV3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=RelA/SpoT family protein {ECO:0000313|EMBL:EKX92261.1};
GN ORFNames=HMPREF9999_00805 {ECO:0000313|EMBL:EKX92261.1};
OS Alloprevotella sp. oral taxon 473 str. F0040.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=1035197 {ECO:0000313|EMBL:EKX92261.1, ECO:0000313|Proteomes:UP000010460};
RN [1] {ECO:0000313|EMBL:EKX92261.1, ECO:0000313|Proteomes:UP000010460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0040 {ECO:0000313|EMBL:EKX92261.1,
RC ECO:0000313|Proteomes:UP000010460};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-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}.
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:EKX92261.1}.
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DR EMBL; AMEK01000044; EKX92261.1; -; Genomic_DNA.
DR RefSeq; WP_009436762.1; NZ_KB290710.1.
DR AlphaFoldDB; L1MMV3; -.
DR STRING; 1035197.HMPREF9999_00805; -.
DR PATRIC; fig|1035197.3.peg.661; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_10; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000010460; Unassembled WGS sequence.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
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; 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; 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; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010460}.
FT DOMAIN 56..156
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 403..464
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 749 AA; 84776 MW; 6297CD52D720DFEF CRC64;
MTQEIQDEAL IQSAFQKLID TYLASPHRKK TEIITKAFNF AKAAHRGVRR RSGEPYILHP
IAVAQVCCEE MGMGSTTICA ALLHDVVEDT DYTRDDIANL FGEKIANIVE GVTKVSGGLL
GNRASMQAET FKKILLTMSD DIRVILVKIA DRLHNMRTLS SMLPSRQYKI VGETLYIFAP
LADRLGLNRI KTELEDLSFK YEHPDDYNAV MQHLKDSKLE RDDAINDFTP AIRAALDSRG
IDYELKARIK SPYSIWQKMQ RKHVPFEEVF DILAIRIIFH PKERDNEIAE CYAIYAALTQ
IYKPHPSRFR DWLSTPKANG YQALHNTFMS HQGKWIEVQI RSDRMDDIAE GGFAAHWKYK
SPDTEVEERE LDTWVNSIKE ILDDPQPDTL DLLDTIKLNL FASELNVFTP KGDILTLPQG
ATVLDFAFAI HSMVGSHCIG GKVNHRLVPI SHRLANGDQI EILTSQSQTI QPDWLNFVTT
GKARGRISAA LRRAARECQR KGESILHEFF KAHELEDNDS NIHKIRSHHH FDTPSALYHA
LGEGRLVLSD ADVQHLLGKK PSRGWGWRRF VPFLKDKSLP ENLEAQSALD ANFVEQLDRK
ATLTLSDEVI SHCEICPHCR PIKGDEVMGY INNNHHLELH RRDCSVALKH KTSFGNNIIA
TVWDNSRPSV HLYEATIHVE GIDSPSVLQE IALVFSQHPQ YQLQSIQLKA HDGIFHGTLG
IRIASTIEVQ ALCSLLLSAG QITKVNRGN
//
