ID A0A1G2B4T4_9BACT Unreviewed; 512 AA.
AC A0A1G2B4T4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=A3F54_03795 {ECO:0000313|EMBL:OGY84193.1};
OS Candidatus Kerfeldbacteria bacterium RIFCSPHIGHO2_12_FULL_48_17.
OC Bacteria; Candidatus Kerfeldbacteria.
OX NCBI_TaxID=1798542 {ECO:0000313|EMBL:OGY84193.1, ECO:0000313|Proteomes:UP000176952};
RN [1] {ECO:0000313|EMBL:OGY84193.1, ECO:0000313|Proteomes:UP000176952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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:OGY84193.1}.
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; MHKD01000017; OGY84193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2B4T4; -.
DR STRING; 1798542.A3F54_03795; -.
DR Proteomes; UP000176952; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR045006; CHLI-like.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR004482; Mg_chelat-rel.
DR InterPro; IPR025158; Mg_chelat-rel_C.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR Pfam; PF13541; ChlI; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF13335; Mg_chelatase_C; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 218..401
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 512 AA; 56612 MW; 35733ABF7CB33852 CRC64;
MSTTTLFSMA FYGLRGQLIT VEVDISAGMP MCTIVGLPDT AVQEAKERVR AALKNMDCRF
PPQRITVNLA PADVRKNGGL YDLPMALGIY AAQNPKFILP QDTIFIGELA LDGSLRAIQG
AIVATQTAKE LRFRAIVLPR DNAAEAGLIH GIEVFPLAHL RDVFHWVQKR DDFTPFVTPH
GTPTDALSSS TTTAALLDFT QIRGQEMAKR ALTIAAAGGH NVLMSGPPGS GKTLLAKSLI
SLLPQLSQQE MIEVTRLYST AGQLNNQRAL ISERPFRNPH HTSSAIALVG GGTWPRPGEL
SLAHRGVLFL DELPEFPRHV LETLRQPLED KTVTIARAHG SIQYPANMIF IATQNPCPCG
YLDDPTHECQ CSAADIKRYR QKISGPLLDR IDLHIHVPKV DTKSLLNQQE PLPEQVIARL
RQRIAHARAL QQQRWPTHSG RLNSDMNQTE IKKWIPINPS LETLLHRAVD NLHLSARALF
RVLRVARTIA DLDAACEVTK DHVAEALQYR AR
//