ID C6VV28_DYAFD Unreviewed; 513 AA.
AC C6VV28;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:ACT94851.1};
GN OrderedLocusNames=Dfer_3646 {ECO:0000313|EMBL:ACT94851.1};
OS Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 / KCTC
OS 52180 / NS114).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT94851.1, ECO:0000313|Proteomes:UP000002011};
RN [1] {ECO:0000313|EMBL:ACT94851.1, ECO:0000313|Proteomes:UP000002011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC {ECO:0000313|Proteomes:UP000002011};
RX PubMed=21304649; DOI=10.4056/sigs.19262;
RA Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL Stand. Genomic Sci. 1:133-140(2009).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP001619; ACT94851.1; -; Genomic_DNA.
DR RefSeq; WP_015813095.1; NC_013037.1.
DR AlphaFoldDB; C6VV28; -.
DR STRING; 471854.Dfer_3646; -.
DR KEGG; dfe:Dfer_3646; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_0_10; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000002011; Chromosome.
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:UP000002011}.
FT DOMAIN 214..397
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 513 AA; 56614 MW; BDC535D383585755 CRC64;
MLAKTYGSAV FGVDATIITI EVNVGQGLGF YMVGLADNAV KESQQRVEAS LKHFGYKMPR
QKLVVNLAPA DIRKEGSAYD LPIAICTLQC SDQLVCVRNT EDYIILGELS LDGILRPIKG
VLPIAIEARK QGFKGIVLPA ENAHEAAIVN NLDVIPVGTL AEAVGYFKGT HEIEPLRVDT
RDLFFTSQND YEADFEHVQG QENIKRALEI AAAGGHNAIM IGPPGAGKTM LAKRIPGILP
PLSLPEALET TKIHSVAGRL GKQATLVSRR PFRSPHHSIS DVALVGGGSY PQPGEISLAH
NGVLFLDELP EFKRSVLEVM RQPLEERKVS ISRAKMAVEY PANFMLIASM NPCPCGYYNH
PERECVCGPG VVQKYLNKIS GPLLDRIDLH VEVTPVSFEQ ISSTRKSESS EQIRERVINA
RERQTERFKN HKEIYSNAMM TPEMVKQICT VNEGGKMLLH KAMERLGLSA RAYDRILKVS
RTIADLADSD DIKVEHLAEA IQYRSLDREN WAG
//
