ID B1V8V0_PHYAS Unreviewed; 706 AA.
AC B1V8V0;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Putative IMP dehydrogenase/GMP reductase {ECO:0000313|EMBL:CAM11383.1};
GN OrderedLocusNames=PA0048 {ECO:0000313|EMBL:CAM11383.1};
OS Phytoplasma australiense.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrXII (Stolbur group).
OX NCBI_TaxID=59748 {ECO:0000313|EMBL:CAM11383.1, ECO:0000313|Proteomes:UP000008323};
RN [1] {ECO:0000313|EMBL:CAM11383.1, ECO:0000313|Proteomes:UP000008323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18359806; DOI=10.1128/JB.01301-07;
RA Tran-Nguyen L.T., Kube M., Schneider B., Reinhardt R., Gibb K.S.;
RT "Comparative genome analysis of 'Candidatus Phytoplasma australiense'
RT (subgroup tuf-Australia I; rp-A) and 'Ca. Phytoplasma asteris' strains OY-M
RT and AY-WB.";
RL J. Bacteriol. 190:3979-3991(2008).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM422018; CAM11383.1; -; Genomic_DNA.
DR AlphaFoldDB; B1V8V0; -.
DR STRING; 59748.PA0048; -.
DR KEGG; pal:PA0048; -.
DR eggNOG; COG0465; Bacteria.
DR eggNOG; COG4942; Bacteria.
DR Proteomes; UP000008323; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000008323};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 313..448
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 51..160
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 526..553
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 706 AA; 83385 MW; 35010660B6FF6C3F CRC64;
MKLKNKIYLS FLSLFGLILL ILFIVGISKT EPKSKSSTTP TITQPPNTQL DTEAKEELNK
LQKRLKDLEI INQQNINNNK KLIEEDNQLS QQINSNLEKI KTLNLQINNL NQELDQKSKE
LNNKETNLND ETKSQLETEI KNLIQKIADL SKQREQINEA TQPLTKKRVE NTKSQVNNKK
LIESIQSETN QTTQFKTIYQ KISDLQQAIN YNNANKENIK ELIIKHQDNP QEVQNLKSYD
LFLDGQLIQF DKQIKQLQNE IEAIKSPNIE KIAKKQITFK DVYGMESEKE ELEDLIFYFK
ESNNNLVNFD KIRPKGYLLY GPPGTGKTFL LKALSNECNA YFIEFEPSKL DKTYVGEGVE
EWEKIWMEAE RHDKTIIFID EISGMANRED KNSNKTSINI VNNILTKLDG FNRSDKKIVL
MGATNHIDQI DKALRSRFSK EIKIDLIKDE EIEGFLKFLI EPYQISYHTY LHLKEIANRC
KGKNYSNRDL TTIINDAYNK TNKFKTLNPK HEVMLPSDLD EVIDTKQRIN KSITEIKARR
KECEEQYESW KQGFLKYLKP PKDTTKIDKH YVFYNLNGLG RGQHREYEPN DIMPFMKNPF
EKWEVKDSSI DFFNTFHTRN KRKDSQFNNM FINDPSNYYT ELNYKGPKWL IEEDKDFFMD
EVQCHIINPK DSRYPKDEKK NYYLHFNPKQ RYITLYTKKF NTKDRL
//