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Database: UniProt
Entry: Q89WL7_BRADU
LinkDB: Q89WL7_BRADU
Original site: Q89WL7_BRADU 
ID   Q89WL7_BRADU            Unreviewed;       512 AA.
AC   Q89WL7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Bll0661 protein {ECO:0000313|EMBL:BAC45926.1};
GN   OrderedLocusNames=bll0661 {ECO:0000313|EMBL:BAC45926.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC45926.1, ECO:0000313|Proteomes:UP000002526};
RN   [1] {ECO:0000313|Proteomes:UP000002526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000313|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR   EMBL; BA000040; BAC45926.1; -; Genomic_DNA.
DR   RefSeq; NP_767301.1; NC_004463.1.
DR   RefSeq; WP_011083488.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89WL7; -.
DR   STRING; 224911.AAV28_00140; -.
DR   EnsemblBacteria; BAC45926; BAC45926; BAC45926.
DR   GeneID; 64020523; -.
DR   KEGG; bja:bll0661; -.
DR   PATRIC; fig|224911.44.peg.30; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_1_5; -.
DR   InParanoid; Q89WL7; -.
DR   OrthoDB; 9813147at2; -.
DR   PhylomeDB; Q89WL7; -.
DR   Proteomes; UP000002526; Chromosome.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002526}.
FT   DOMAIN          209..393
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   512 AA;  53656 MW;  7070838E97A17C20 CRC64;
     MVQRVSTVAF EGIEARAVDV QVQVAPGLPA FAIVGLPDKA VSEARERVRS ALIASGLALP
     ARRIIVNLAP ADLPKEGSHY DLPIALGLMA AIGAIPPDAL TGFTVLGELG LDGSIAPVAG
     VLPAAIGANV REEGLICPAA CGSEAAWASP DIQIIAAQSL IQIANHFKGT QVLSRPSPKV
     HEAAASKLDL RDIKGQESAK RALEIAAAGG HHLLMIGAPG AGKSMLAARL PSILPPLSPG
     ELLEVSMIAS VAGEIEGGAL TARRPFRSPH HSASMAALTG GGMRAKPGEI SLAHQGVLFL
     DELPEFDPRV LDSLRQPLEN GEVSVSRANH RVTYPARFML VAAMNPCRCG NAFEPGYACK
     RGRIDRCTGD YQARISGPLM DRIDLRIEVP AVTAADLILP PPAEGSAEVA ARVAAARDIQ
     LARYADIGLP NVRTNAEAPA SVLEDIAKPD AQGAKLLRDA AETMRLSARG YHRVLRVART
     LADLDGADKI GRLHLAEALS YRALAEDVRQ MA
//
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