ID A0A1G2NCX7_9BACT Unreviewed; 525 AA.
AC A0A1G2NCX7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=A2938_02705 {ECO:0000313|EMBL:OHA33910.1};
OS Candidatus Taylorbacteria bacterium RIFCSPLOWO2_01_FULL_48_100.
OC Bacteria; Candidatus Taylorbacteria.
OX NCBI_TaxID=1802322 {ECO:0000313|EMBL:OHA33910.1, ECO:0000313|Proteomes:UP000177797};
RN [1] {ECO:0000313|EMBL:OHA33910.1, ECO:0000313|Proteomes:UP000177797}
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:OHA33910.1}.
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; MHSA01000021; OHA33910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2NCX7; -.
DR Proteomes; UP000177797; 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 228..409
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 525 AA; 57156 MW; CF078877060FBE8B CRC64;
MSFAKVWSAE THLLTPHLIS VEADIAGGLH SFSVVGLPDK AVEESRDRVS AAIKNSGFKS
PKQKNQKVTI SLAPADLKKE GPAFDLPVAL AYLKAVGAIR FAPEKKLFLG ELSLDGELRP
VAGVLPLVEE ARKRDFEEVF VPQGNAREAA LIRGIQVYAA PTLTAVIAHL IPKDLAGDGD
ETPFVKKRAL KQVHETAIPD EPPEAQIDLS DIKGQETAKR GLEIAAAGGH NILLWGPPGT
GKTMLAKAFA GLLPPLSFQE MLEVTGIHSV AGKLRDTIVS HPPVRSPHHT SSYVSITGGG
AIPKPGEATL AHRGVLFLDE FPEFDRRVID TLREPLEERM ISVSRARGSA HFPAHFILIA
AMNPCPCGNK GVKGKSCVCG ANAAERYRRK ISGPVIDRID LAIEVSAVEY GKLSDEARDG
SESKEVRERV IAARKRQEER FKKAKLKAKT NADTPAKHIA RIIPLDEKTK GMLNANARRL
DLSARSYHRV MKLARTIADL AERDEVTEDD ILEALSYRPK QIINQ
//