ID A0A0A6Y2B7_9FLAO Unreviewed; 511 AA.
AC A0A0A6Y2B7;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KHE69577.1};
GN ORFNames=HMPREF9074_08310 {ECO:0000313|EMBL:KHE69577.1};
OS Capnocytophaga sp. oral taxon 329 str. F0087.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE69577.1, ECO:0000313|Proteomes:UP000030579};
RN [1] {ECO:0000313|EMBL:KHE69577.1, ECO:0000313|Proteomes:UP000030579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0087 {ECO:0000313|EMBL:KHE69577.1,
RC ECO:0000313|Proteomes:UP000030579};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2014) 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:KHE69577.1}.
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DR EMBL; AFHP02000103; KHE69577.1; -; Genomic_DNA.
DR RefSeq; WP_009391773.1; NZ_KN390004.1.
DR AlphaFoldDB; A0A0A6Y2B7; -.
DR STRING; 706436.HMPREF9074_08310; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_0_10; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000030579; 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; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 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}.
FT DOMAIN 213..395
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 511 AA; 57033 MW; 53364BDA17161774 CRC64;
MLVKIYGSAV FGVEATTITI EVNIDKGVGY YLVGLPDVAI KESNYRIAAA LQNNGYKIPG
RKITINMAPA DMRKEGSSYD LSLAIGILAA NEQIQADDLD KYIIMGELSL DGGLQPIKGA
LPIAIQARKE GFKGFILPAQ NAKEAAIVDQ LEVYGVENIK DVIAFFNGER QLERTIIDTR
KEFYKNLEFP EFDFADVKGQ ETVKRCMEIA AAGGHNIILI GPPGSGKTML AKRLPSILPP
MTLHEALETT KIHSVVGRIK DSGLMSHRPF RSPHHTISDV ALVGGGTYPQ PGEISLAHNG
VLFLDELPEF KRAVLEVMRQ PLEDREVTIS RAKFSITYPA SFMLVASMNP SPSGYFNDPD
APMSSSPAEM QRYMSKISGP LLDRIDIHIE VNPVPFEKLS DERKAESSSE IRKRVIEARN
IQTERFKEYE HIHYNAQMNT KQIQKFCKVS EESLKLLKNA MTRLNLSARA YDRILKVART
IADLEKTEKV EPHHIGEAIQ YRSLDRDGWF S
//
