ID A0A1Q7HVF8_9CHLR Unreviewed; 649 AA.
AC A0A1Q7HVF8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=AUH85_09305 {ECO:0000313|EMBL:OLC55412.1};
OS Chloroflexi bacterium 13_1_40CM_4_68_4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC55412.1, ECO:0000313|Proteomes:UP000185706};
RN [1] {ECO:0000313|EMBL:OLC55412.1, ECO:0000313|Proteomes:UP000185706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
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:OLC55412.1}.
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DR EMBL; MNFM01000095; OLC55412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7HVF8; -.
DR Proteomes; UP000185706; Unassembled WGS sequence.
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; 1.
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; 1.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 70737 MW; 1F4271CAC21176E9 CRC64;
MTTTTTPAPT TSHPATYMNA PVPAVPETPT RRFLLTSAYV LEHNLRRLII LAVIVAVAVS
LYGVRGIFQG ILDMIGQAPQ LLVLLLFYSF MMIVQFGALM WFMSRPRTYT VTPDSPQIGL
TFENYRGQPD LLDHAKSLVR ILKGVKTFQQ RGGEMPAGML LAGPPGTGKT FLAGCMAAEA
NLPFIYVDAS SLSSMWMGVD ALIVISLFRK ARGLARKYAA PGQPGCCILF LDELDSVGLS
RGGMSGGQQQ GMMGPMGMMG GRGLALNTML NQMDSLGKHV EDRFKHKIGR WLGVIRGPVP
PKPVVFVIGA TNRPDVLDPA LVRAGRLDRK LMVYVPDGDG RKDIIQHYLG TKAHDPEMPV
ELMVGDSIGW TPIDIKTIIN ESLIVAHDDG REFFTYRDWL VARDARMLGI KQPIQTMSAP
DRRAIAYHEA GHAVAARYLQ QENRIQKASI IRMGDALGVV QRSSREERYT RHAREIETDI
MVSLASRAVE EVYLGTKMSG AGSDLQTATY LAMSYIGSLG MGPTLLTMPG SGMMTPPGPV
LKLADKLLDE LYEETKRLVR EKEYAVHAIA GALAQKGELI GPELEEIFET ADLSNPEAAK
PFERKPIALP KMSEDWGEKD GEKFAEAVAA AVAAQAAGAA KKQAGPTKK
//