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Database: UniProt
Entry: A0A1G2B4T4_9BACT
LinkDB: A0A1G2B4T4_9BACT
Original site: A0A1G2B4T4_9BACT 
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}.
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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
//
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