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Database: UniProt
Entry: A0A0Q6F913_9ACTN
LinkDB: A0A0Q6F913_9ACTN
Original site: A0A0Q6F913_9ACTN 
ID   A0A0Q6F913_9ACTN        Unreviewed;       539 AA.
AC   A0A0Q6F913;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:KQT91085.1};
GN   ORFNames=ASG49_12130 {ECO:0000313|EMBL:KQT91085.1};
OS   Marmoricola sp. Leaf446.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Marmoricola.
OX   NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT91085.1, ECO:0000313|Proteomes:UP000051542};
RN   [1] {ECO:0000313|EMBL:KQT91085.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT91085.1,
RC   ECO:0000313|Proteomes:UP000051542};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT91085.1, ECO:0000313|Proteomes:UP000051542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf446 {ECO:0000313|EMBL:KQT91085.1,
RC   ECO:0000313|Proteomes:UP000051542};
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:KQT91085.1}.
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DR   EMBL; LMRF01000004; KQT91085.1; -; Genomic_DNA.
DR   RefSeq; WP_056542217.1; NZ_LMRF01000004.1.
DR   AlphaFoldDB; A0A0Q6F913; -.
DR   STRING; 1736379.ASG49_12130; -.
DR   Proteomes; UP000051542; 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:UP000051542}.
FT   DOMAIN          226..415
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          280..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   539 AA;  57704 MW;  507F4071E56DA4C5 CRC64;
     MVATTHTVSL QGTVGHVVDV QVDLAAGVVG TSLVGRPDTS INEARDRCKA AIGNTVFDSD
     KRRWPNTRRV TILLSPTDLP KRGPHFDLAI AVAVLAAADP TIPAAALRGT ALVGELTLDG
     RVRCVPGVLP MVMAAAARGI HTVFVPEPQV EEARMVEGLS VFGIRSLGQT VALLAGEEVP
     DAPPVEAMTG SPLLTWRGEQ RLDDLDLADV LGIPDTRYAV EVAAAGGHHL LLTGPKGSGK
     TTIAERIPGL LPDLTDAESL ELTAVHSLCG SLPPGSTRIT RPPFRNPHHS ASRSGILGGG
     TGRVRPGDVS KAHLGVLFLD EFPLFPSDVV DALREPLEAG EISISRGEDD ATFPARAMFV
     FASNPCRCGE YHPWARDHRC TCSEQARREY RAKVSGPVAD RIDITRFVEP VRDGSAGSLP
     FERPESSAEV RVRVAAARDR QGERYAGLPW RLNAHAPGPA LREEWPLAPL AAARLEDEVM
     RTRLTRRGAV RAHRVAWSVA DLAGLERPGP EELDVALRLR SAAPLLMGSL PRMVRGRTA
//
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