ID A0A1G2E2T9_9BACT Unreviewed; 517 AA.
AC A0A1G2E2T9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=A2494_02690 {ECO:0000313|EMBL:OGZ20157.1};
OS Candidatus Lloydbacteria bacterium RIFOXYC12_FULL_46_25.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798670 {ECO:0000313|EMBL:OGZ20157.1, ECO:0000313|Proteomes:UP000178106};
RN [1] {ECO:0000313|EMBL:OGZ20157.1, ECO:0000313|Proteomes:UP000178106}
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:OGZ20157.1}.
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DR EMBL; MHLU01000029; OGZ20157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2E2T9; -.
DR Proteomes; UP000178106; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 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 219..400
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 517 AA; 56677 MW; F9F36824183FD2A2 CRC64;
MAFATITSAQ ATLLGAQVIT IEADLTKGLH AFTIVGLPDK AVEESRDRVS AAIKNSNWKS
PKQRNQKITI ALAPANLKKE GPAFDLPIAL CYLLATGDII FDPTNKIFIG ELALDGHIRP
IKGALAIASS AKKLGITEVY VPKENAEEAA LVSGITIFPV TSLKELVSHL EEHKPDRATI
TPQEKTLITE IAPATYNGAF LDIRGQETAK RGLMIAAAGG HNIALFGPPG TGKTMLAKAF
NELLPQLSEE ETLEVTAIHS VAGALKQTII THPTFRSPHH TASYVSVIGG GAIPKPGEVT
LAHRGVLFLD EFPEFDKRVI ESLRQPLEDG VVHIARAKGS ERFPAQFMLI AAMNPCPCGY
HGDPKKKCTC TPTSITRYQQ KISGPIIDRI DMWIEVPRLE HATLAPGKRE AGAREQFENF
IKQIVSARAH QSNRFAQFPH IGLNREMSVR DIDTMIKLSP DVLTLLNESA KRLDLSPRAY
HRVIKLARTI ADLDESRHIK EAHIFEALQY RPKRLFA
//