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Database: UniProt
Entry: A0A0Q9KK65_9MICO
LinkDB: A0A0Q9KK65_9MICO
Original site: A0A0Q9KK65_9MICO 
ID   A0A0Q9KK65_9MICO        Unreviewed;       514 AA.
AC   A0A0Q9KK65;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KRE41900.1};
GN   ORFNames=ASG74_05290 {ECO:0000313|EMBL:KRE41900.1};
OS   Knoellia sp. Soil729.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1736394 {ECO:0000313|EMBL:KRE41900.1, ECO:0000313|Proteomes:UP000051965};
RN   [1] {ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|Proteomes:UP000051965};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE41900.1, ECO:0000313|Proteomes:UP000051965}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil729 {ECO:0000313|EMBL:KRE41900.1,
RC   ECO:0000313|Proteomes:UP000051965};
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:KRE41900.1}.
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DR   EMBL; LMSA01000002; KRE41900.1; -; Genomic_DNA.
DR   RefSeq; WP_056139817.1; NZ_LMSA01000002.1.
DR   AlphaFoldDB; A0A0Q9KK65; -.
DR   STRING; 1736394.ASG74_05290; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000051965; 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;
FT   DOMAIN          217..401
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   514 AA;  54101 MW;  64A2B17DA76D73D6 CRC64;
     MSAKLGRTLC VALSGLEGRL VDVEAHISSQ LPNFSVTGLP DKACGQAPDR VRSAAATSGC
     PLPPQRITVN LSPASIPKQG TGFDIAIALA VLAASGAVDA RRIAQVVHLG ELGLDGRVRG
     VRGILPAVLA AARAGVRHVV VPPENVAEAQ LVDGVTVHCA PTLATLVHWY AARGGVDPLP
     VAGAVSEQAE ATARRGDLAD VVGQPEARLA VEMAAVGGHH LLMNGPPGVG KTMLAERLVT
     ILPPLSREQA LQTHAIRSLT GDEIRASELD LTPPFVAPHH SASMASITGG GSGVVLPGAI
     SRAHCGVLFL DEAGEFKTSV LQQLRQPLES GEVTIARAKQ LVRYPARFQL VLATNPCPCG
     RAWGKGIDCM CSAVELRSYQ AKLSGPLIDR VDIQVVVPPV SRAAFGDEVG ESSEVVLERV
     LRARAVQRER WSRHGWTTNS RVPGHALRRR PWRLPSGATA SIDRALDLGQ LTLRGYDRTV
     RLAWSAADLF GRVSPTAEDV GLAFTLRSQG RAAA
//
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