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Database: UniProt
Entry: B6GBZ6_9ACTN
LinkDB: B6GBZ6_9ACTN
Original site: B6GBZ6_9ACTN 
ID   B6GBZ6_9ACTN            Unreviewed;       510 AA.
AC   B6GBZ6;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-NOV-2023, entry version 55.
DE   SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:EEA90260.1};
GN   ORFNames=COLSTE_01615 {ECO:0000313|EMBL:EEA90260.1};
OS   Collinsella stercoris DSM 13279.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Collinsella.
OX   NCBI_TaxID=445975 {ECO:0000313|EMBL:EEA90260.1, ECO:0000313|Proteomes:UP000003560};
RN   [1] {ECO:0000313|EMBL:EEA90260.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90260.1};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Collinsella stercoris (DSM 13279).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEA90260.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13279 {ECO:0000313|EMBL:EEA90260.1};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) 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:EEA90260.1}.
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DR   EMBL; ABXJ01000083; EEA90260.1; -; Genomic_DNA.
DR   RefSeq; WP_006721249.1; NZ_DS995476.1.
DR   AlphaFoldDB; B6GBZ6; -.
DR   STRING; 445975.COLSTE_01615; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_0_11; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000003560; Unassembled WGS sequence.
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:UP000003560}.
FT   DOMAIN          210..392
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   510 AA;  53649 MW;  B2DF15FE045462F5 CRC64;
     MSARCATFAV HAACLRGVEA FGVTVEVSAS GTIPSLTIVG MADAAVMEAR SRIRCALRSS
     GFDVPRCALT VSLAPGDIRK TGSGLDLPIA VAILALTGQI PVNGLDGCLF VGELALDGGI
     CSVRGEVAYQ LLAREQGLAY IGGATDGHVS IQGTDAWRLD DLARLKDGIE QARRPYRAPA
     PRPAPELMLD FSDVCGQEIA KRGIAVAATG ELGLMMIGAP GSGKTMLAKR MTGILPAIED
     RELQEALCVH SVAGEPVDGL LRGTRPFRSP HHSISAAGLV GGGRPVRPGE ISLAHGGVLY
     LDELGEFPSN TLQMLRQPLE DGSVRIVRVD GAYLLPARFQ LVAASNPCPC GYLGDRDVAC
     RCSDAAIERY QAKLGGPLAD RIDIVLHIAR PDPSLIIEGA EGLSTKELAD MVRRGRAFRA
     SRERARGGPA QGSLSLESSL APALIDSEAR EVMLEIAKRT NLTGRGIARL ARIARAIADL
     EEADRVDVAH VLEASQLQGR RDVGGGYGQV
//
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