ID A0A1Q7UM54_9CHLR Unreviewed; 646 AA.
AC A0A1Q7UM54;
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=AUG82_10265 {ECO:0000313|EMBL:OLE01850.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE01850.1, ECO:0000313|Proteomes:UP000186213};
RN [1] {ECO:0000313|EMBL:OLE01850.1, ECO:0000313|Proteomes:UP000186213}
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:OLE01850.1}.
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DR EMBL; MNIY01000191; OLE01850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7UM54; -.
DR STRING; 1805225.AUG82_10265; -.
DR Proteomes; UP000186213; 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 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 137..308
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 581..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 71190 MW; FD38EDBE81E4D39D CRC64;
MAENTKAKAK KSSLDRSIDL GMDQFGRFVR LRWFWLVVVS IIIWYTFVFV VPQLSAPSPG
SILYYAFQIS FALLFGIMQF VAIFWFLGRP RLYWVMPGET GVTFEDYKGN PEVLEAARRI
VGLLRGVKEF QQMGGSPVRG LLLSGPPGTG KSYLAQCMST EAGVPFAYAS AASFRAMFIG
MDILMIRRLY SKARRLAREY GGCVVFMDEI DAIGASRGGG GMGLGGGMMG LMGGAGTGGL
NQLLMEMDPP NIETGWFKKI LRTIGLTHSR VQTEPVLTVA ATNIPESLDR ALLRPGRFDR
KIHVAPPTDK YRAEVILYYL NKVEHDPDIS INALVQRLVD YTPVAIKHVI NEAVIIAHFD
GRDKITYKDL IEAQDVHEFG LRQTSELTPI DRRRLAYHEA GHAVASYYLY ERYFPAYVTI
HQRSDLEGAA AFALPRPKES IKTLSKEDIL QRIQVALAAR ATEELFLDLN MNGVSSDLQQ
ATTNAFAYVG LWGMDGTLAS ARVVEVPQTK LDERVEKLLQ SQFKAVKNLL QDHKEALIAV
AEALIEHDEL VAEEIKQLID EADARKVTRV VLSDFEAILG TGNGHSNGNG KNGYALTGGN
GNGNVPAGDS PRIGSTPSTS SLPPSNEVTS IEQVFTDEDA PPFIDK
//
