ID A0A0B7IVJ4_9PROT Unreviewed; 743 AA.
AC A0A0B7IVJ4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Bifunctional (P)ppGpp synthetase II and guanosine-3',5'-bis pyrophosphate 3'-pyrophosphohydrolase {ECO:0000313|EMBL:CEN55092.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:CEN55092.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:CEN55092.1};
GN Name=spoT {ECO:0000313|EMBL:CEN55092.1};
GN ORFNames=BN1209_0031 {ECO:0000313|EMBL:CEN55092.1};
OS Candidatus Methylopumilus turicensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylopumilus.
OX NCBI_TaxID=1581680 {ECO:0000313|EMBL:CEN55092.1, ECO:0000313|Proteomes:UP000056322};
RN [1] {ECO:0000313|Proteomes:UP000056322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-10A-171 {ECO:0000313|Proteomes:UP000056322};
RA Salcher M.M.;
RL Submitted (DEC-2014) 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; LN794158; CEN55092.1; -; Genomic_DNA.
DR RefSeq; WP_045750434.1; NZ_LN794158.1.
DR AlphaFoldDB; A0A0B7IVJ4; -.
DR STRING; 1581680.BN1209_0031; -.
DR KEGG; mbac:BN1209_0031; -.
DR HOGENOM; CLU_012300_3_0_4; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000056322; Chromosome 1.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:CEN55092.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000056322};
KW Transferase {ECO:0000313|EMBL:CEN55092.1}.
FT DOMAIN 71..170
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 412..473
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 660..735
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 743 AA; 83426 MW; F1B1822724394C8C CRC64;
MPNDKNHHAG KRAADFLKPA APLLPADRED SQLTLALKKY LKPSDIEQVW EAYRFGDAAH
QGQIRKSGEP YITHPVSVAL ILAGLHLDTP TIIAALLHDV VEDTGITKEE VSEKFGTQVA
ELVDGLSKLD KIEFQSATEA QAENFRKMLL AMSQDVRVIL VKLADRLHNM QTLDVMKPDK
RRRIARETLE IYAPIANRLG LNEIYQELED LSFKNHYPMR YEVLSKAILA ARGNRKEVVG
KILDAIKGRL AEMKIEADVS GREKHLYSIY KKMTGKTIAF SQIFDIYGFR LIVKDLPSCY
AVLGVLHGLY KPIPGKFKDY IAIPKANGYQ SLHTTLFGPF GTPIEIQIRS QEMHNIADAG
VAAHWLYKTT DADFTAMQQQ THQWLQRLLD IQSESADSLE FLEHLKVDLF PDEVYVFTPK
GKILALSKGA TAVDFAYAVH TDIGNRCVAV KINQELAPLR SELRNGDHVE IITAAHAHPN
PAWLNYVVSG KARAHIRHFL KSMQSTESAH LGERMLNQAL RALHTDASKI DESQWQKLLR
DYGAKNKEEI LTDIGLGKRL NVMVAHQLIA MGEEHGERHA KHPNKPLGTI TIRGSEGMAV
QFAQCCRPIP GDPILGFINK DRGLVIHTHD CPSIRKFRVD PDKWLDVEWD PQGNRLFKVN
LKIAAANKPG MLATIASAIA DANSNIDNIS MEESDNSTYT NILFTVQVQD RVHLADLMRR
LRKIPDVVRM NRTKGTGAEQ RAQ
//
