ID R7BKC0_9FIRM Unreviewed; 505 AA.
AC R7BKC0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Mg chelatase subunit ChlI {ECO:0000313|EMBL:CDD65588.1};
GN ORFNames=BN803_02308 {ECO:0000313|EMBL:CDD65588.1};
OS Firmicutes bacterium CAG:882.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1262991 {ECO:0000313|EMBL:CDD65588.1, ECO:0000313|Proteomes:UP000017928};
RN [1] {ECO:0000313|EMBL:CDD65588.1, ECO:0000313|Proteomes:UP000017928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:882 {ECO:0000313|Proteomes:UP000017928};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDD65588.1}.
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DR EMBL; CBHL010000086; CDD65588.1; -; Genomic_DNA.
DR AlphaFoldDB; R7BKC0; -.
DR Proteomes; UP000017928; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032508; P:DNA duplex unwinding; 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; IPR001208; MCM_dom.
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 PRINTS; PR01657; MCMFAMILY.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017928}.
FT DOMAIN 208..389
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 505 AA; 55156 MW; C3F47B20A440C0C4 CRC64;
MVSKVGCAMV TAAGASLLEV EADVSGGLPD IEMTGNLSVS VKDGRERIRV AIKKCGFPFP
QGRVTINIAP AALRKEGSGF DLAVACAILE EIGIVDEEKL NGRIVVGELG LDGSVIGVRG
VLPIVLAAYK AGYIGCVVPA DNYEEASMVS DIEITPVEHL SQLAGSEFGI IMPKRADINR
KKDESRLDYS DISGQDYAKK AILTAAAGRH NILLMGPPGA GKTMLASRIP TIMPEMSEQE
RLELACLYSI AGKLGDGGNM GIRPFRAPHH SITTAALAGG GRTIEPGEVS LASKGVLFLD
ELTRYDTRVI EQLREPLESG KIMINRVSGS YELPADFMLV AAMNPCACGF YPDRTRCRCT
AWEVNRHYGR ISRPILDRID ISVVLQRVNY DELTGRAKEK KRGCSSRDMR EIVERVWSIQ
SDRLGEGRSN GRMTNDEIKK YCVLDAQSEK LVREAYEHYG LSARAYHKLL KVARTLADID
GAERIAQEHI LEALSYRVKD KGDEQ
//
