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Database: UniProt
Entry: A0A0Q9CFK6_9CELL
LinkDB: A0A0Q9CFK6_9CELL
Original site: A0A0Q9CFK6_9CELL 
ID   A0A0Q9CFK6_9CELL        Unreviewed;       512 AA.
AC   A0A0Q9CFK6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KRD40404.1};
GN   ORFNames=ASE27_05775 {ECO:0000313|EMBL:KRD40404.1};
OS   Oerskovia sp. Root918.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Oerskovia.
OX   NCBI_TaxID=1736607 {ECO:0000313|EMBL:KRD40404.1, ECO:0000313|Proteomes:UP000051694};
RN   [1] {ECO:0000313|EMBL:KRD40404.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD40404.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD40404.1, ECO:0000313|Proteomes:UP000051694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root918 {ECO:0000313|EMBL:KRD40404.1,
RC   ECO:0000313|Proteomes:UP000051694};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRD40404.1}.
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DR   EMBL; LMJG01000011; KRD40404.1; -; Genomic_DNA.
DR   RefSeq; WP_056648679.1; NZ_LMJG01000011.1.
DR   AlphaFoldDB; A0A0Q9CFK6; -.
DR   Proteomes; UP000051694; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051694}.
FT   DOMAIN          216..400
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   512 AA;  53116 MW;  105CBC7C2367AE83 CRC64;
     MTLGTTFAVS LVGLSGHLVE VQAHLAASVP GFTLVGLPDA ALSESRDRVR AAIASSGISW
     PQRKVTVNLS PASLPKSGSG FDLAIAVAML AGARRISVSD PEKVVHIGEL GLDGRLQPVR
     GVLPAVAAAV AAGLCDVVVP LEDAQEARLV PGARVVGVAS LAEVAALYGA EVPGMVLPSA
     ASRAPRVERP RRAEGDLRDV LGQEQARRAV EVAAAGGHHL LLVGPPGAGK TMLASRITSI
     LPDLDEAEAV EVTAVHSVAG VFDPGQGLVR RPPYEDPHHT ATAASIVGGG SGLPRPGAAS
     RAHRGVLFLD EAPEFGSRVL QTLRQPLEHG ELVIHRAAGS ARYPARFQLV LAANPCPCGL
     SIGKGIECQC TPIVRRRYFG RLSGPLLDRV DVQVEVRPVT RVDRAGEGDV ETSATVAVRV
     ADARAAAKAR LAGTPWSTNA EVPGTWLRER LGAGRGLLAD VDTALDRGTL SLRGADRVLR
     LAWTVADLAG RAAPTRSDVG QGLALRTRGH HG
//
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