ID Q0RE07_FRAAA Unreviewed; 793 AA.
AC Q0RE07;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN OrderedLocusNames=FRAAL5675 {ECO:0000313|EMBL:CAJ64308.1};
OS Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ64308.1, ECO:0000313|Proteomes:UP000000657};
RN [1] {ECO:0000313|EMBL:CAJ64308.1, ECO:0000313|Proteomes:UP000000657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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DR EMBL; CT573213; CAJ64308.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0RE07; -.
DR STRING; 326424.FRAAL5675; -.
DR KEGG; fal:FRAAL5675; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_355142_0_0_11; -.
DR Proteomes; UP000000657; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 205..445
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 86813 MW; 8D1115EE82430735 CRC64;
MKFLILLGAV FLFVVAADVS GDPLMTWADA LRIQARKSAW VLVLFGLEVL HQLHMLIAER
WSAYHVFWTD RVFGRAERRM LRLNDWNRYR LSRAAKWIVA LALALFVYAR LSHTSVFDAL
VQVPGDLWKA IPFVLQIVLL MVLVVGQFVV MFWFLSKGGV DTYFPEDITT RFADVWGQDH
VVSRVQENVF YLERPEEIES RGGHVPGGIL LWGPPGTGKT LIAEAVAGET GKPFVFVDPG
AFSAMFIGVG ILKVKSLFRK LRKLSLRYGG VIVFFDEADT LGSRGALNGG FGGMGNGARS
WFARQGSPAS AAPGGLGGPG AAGRRPDAFG ARDGGVGDLC NGLSYLSSAA RSEITREAAR
EQFVMGGGGG GFDGTLQALL TEMSGLKKPR GFLNRVVRRT LGMRPKPPPK YRILVMMATN
MPQSLDEALL RPGRIDRQYK VGYPSKEGRI RTFEGYLAKV RHELTPEQIE RLAIMSPEST
GATIKDTVNE ALVQAVKDGR EVITWQDILR ARVIKEYGLA DDHEHIDRER HSIALHEACH
AVVAYRMQRG RVIDLATIER RGGVGGFVAH VAVEDRMFMW KSEIEIQVMV SLASLAGERM
FFEGDNTVGV GGDLRSATLL VANFISSAAM GETLASRLSM LEQQMGNASI DADRPFGEQV
EVKLRELYER TEAVLGANRR EILALTHALE THKTITGEDV EAIMEGRTGP TVDGRRYHEP
DFLNVAERYH SDAVRAHRGQ TRELHKLPEL GRVAASSSVE APGPSSAAPA VAPPVPPAGR
PSAAGQGQEG PGV
//
