ID A0A117LDQ0_9BACT Unreviewed; 504 AA.
AC A0A117LDQ0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 20.
DE SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KUK40298.1};
GN ORFNames=XD68_0172 {ECO:0000313|EMBL:KUK40298.1};
OS Synergistales bacterium 54_24.
OC Bacteria; Synergistota; Synergistia; Synergistales.
OX NCBI_TaxID=1635272 {ECO:0000313|EMBL:KUK40298.1, ECO:0000313|Proteomes:UP000054050};
RN [1] {ECO:0000313|Proteomes:UP000054050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUK40298.1}.
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DR EMBL; LGFQ01000003; KUK40298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117LDQ0; -.
DR STRING; 1635272.XD68_0172; -.
DR PATRIC; fig|1635272.3.peg.1114; -.
DR Proteomes; UP000054050; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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 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;
FT DOMAIN 207..387
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 504 AA; 54112 MW; 3E2CB6D35A626104 CRC64;
MSKALGITLR GIEAVAVEVE VEVTGGLFAI SIVGLPDAAV REAKERVRAA LRSIGISLRG
RIAVNLAPAD LPKEGALLDL PIAIEMAKQV GSVPASSQPA VFVGELALDG RLRRAKGAVP
AAMLARKLSL PLYIPHENAH EVSLVKGVEA YAISHIAELI EALRGEVALR PIEHRVPAPQ
EIEVDVDLAD IKGQAGAKRA MEIAAAGHHN LLMVGPPGSG KTMLARALKS ILPPLSDEEL
LEVLLIYSAR GLSFDGGRAR PFRSVHHTAS TVAVCGGGNA LQPGEISLAH RGVLFLDEFT
EFRRDLIEAM RQPLEDGKIV VSRSSGSVTY PAQVLLALAC NPCPCGNFGD PGFPCRCSPG
ELERYQRKLS GPILDRIDMQ ISVPRLSPDE LMAVEPSGED SASVRRRVER AREIQIERWK
AWGIRSNAEV PEALLRKEAH IKKEARAFLR SAMGRSRLSG RGFTRILRVA RSVADLAGEE
CVGASHVAEA LAYREGANIY GRPS
//