ID A0A1G0YZ34_9BACT Unreviewed; 513 AA.
AC A0A1G0YZ34;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=A2017_04865 {ECO:0000313|EMBL:OGV51200.1};
OS Lentisphaerae bacterium GWF2_44_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798571 {ECO:0000313|EMBL:OGV51200.1, ECO:0000313|Proteomes:UP000176916};
RN [1] {ECO:0000313|EMBL:OGV51200.1, ECO:0000313|Proteomes:UP000176916}
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:OGV51200.1}.
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DR EMBL; MHBF01000083; OGV51200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0YZ34; -.
DR STRING; 1798571.A2017_04865; -.
DR Proteomes; UP000176916; 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 216..398
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 513 AA; 55772 MW; 76D1006F3786CF80 CRC64;
MLAKTYSATV SGIDAYTVEV EINGTEQGEA TFVTIVGLPD AAVRESRDRV RSAMYSMGFN
HPLGATVVNL APADMKKEGA AFDLPIALGM IAVTGKLERQ KLAETMIVGE LALDGSVRAV
KGVLPIAVHA GKMKKISALL VPSANAAEAA IGSGKIPVYA IDNLSDAVSF LNGKSSKTPV
KADIQDALSH NIHYPDFAEV KAQPLAKRAL EISATGGHNV LMIGPPGTGK SMLAKRLSGI
LPPMNIQETL ETSKIHSILG LLSSGAPLLN MRPFRAPHHT ISDAGLLGGG QNPMPGEISL
AHNGVLFLDE MPEFKRNVLE VLRQPLENGN ITVSRAAGSF TYPSRFILIA AMNPCPCGLS
NKEIGCRCKP NEIKRYRSRI SAPLLDRIDI HVEVGQLNED ELLAAPSGET SAQIRQRVIQ
SRKLQELRYK GRGIYCNSQM ESRELQEYCV LNKQNYTLLR HAIKEMNLSA RAYDRILRVS
RTIADLANSP SIEEEHLFEA IQYRALDKNI WKI
//
