ID B7XSM0_BORGR Unreviewed; 667 AA.
AC B7XSM0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase ((PpGpp)ase) {ECO:0000313|EMBL:EED29074.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:EED29074.1};
GN ORFNames=BGAPBR_0198 {ECO:0000313|EMBL:EED29074.1};
OS Borreliella garinii PBr.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=498743 {ECO:0000313|EMBL:EED29074.1, ECO:0000313|Proteomes:UP000006103};
RN [1] {ECO:0000313|EMBL:EED29074.1, ECO:0000313|Proteomes:UP000006103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBr {ECO:0000313|EMBL:EED29074.1,
RC ECO:0000313|Proteomes:UP000006103};
RX PubMed=22123755; DOI=10.1128/JB.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.-G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(2011).
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:EED29074.1}.
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DR EMBL; ABJV02000002; EED29074.1; -; Genomic_DNA.
DR RefSeq; WP_004791832.1; NZ_ABJV02000002.1.
DR AlphaFoldDB; B7XSM0; -.
DR STRING; 29519.BLA33_03320; -.
DR Proteomes; UP000006103; Unassembled WGS sequence.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
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; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
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; 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 Hydrolase {ECO:0000313|EMBL:EED29074.1}.
FT DOMAIN 62..161
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 401..462
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
SQ SEQUENCE 667 AA; 77727 MW; 8988E6627799AE56 CRC64;
MIQAYEIAHL IKINDLEKAK NIFKKTVENT YKDEFERKSI FKALEIAEQL HYGQYRESGE
PYIIHPIMVS LFLAKFQLDF KATIAGLLHD VLEDTNIEKE EIVKEFDEEI LSLIDGVTKI
HDLHNKTRSI KEANTISKMF FAMTHDIRII IIKLADKLHN MTTLSYLPKN RQDRIAKDCL
STYVPIAERL GISSLKTYLE DLSFKHLYPK DYKEIKNFLS ETKIEREKKL YKGKLSIEKE
LQKSGIEAEI TVRSKHFYSI FRKMQTRTNK LTQIFDTLGI RIICKKQKEC YEILEIVHRV
WKPIPGRLKD YIASPKENKY QSLHTTVRIP EDNQLIEIQI RTEEMDRIAN YGVAAHWIYK
EQIALKADDL SFINRIKKWQ QESANKSQYS MNDIHKELLN TFIYVYTPEG EVVELPFGSN
SIDFAYIIHT DIGDQALYAK INGKISSITK PLKNEQIVEI FTSKDSKPDV IWLNSVRTKK
ARSKIRSWLN KNDNTIFVDN NIIAYLVGAN KEQRKLFSLF KAYTKTKIKR IAIDSECNPT
TGEDIVGIIH KDEIIVHNEN CQKLKYYKKN QLIEVEWEAT PTRKVHHIIL LLKELKGIFS
YLENIFTIND VRLISEKIED CGNGHGITNI IVSSNAKNIA KIISALKENP NILQIMQVEE
DIKNYDN
//
