ID C6XXN8_PEDHD Unreviewed; 512 AA.
AC C6XXN8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:ACU02292.1};
GN OrderedLocusNames=Phep_0066 {ECO:0000313|EMBL:ACU02292.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU02292.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU02292.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(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; CP001681; ACU02292.1; -; Genomic_DNA.
DR RefSeq; WP_012780245.1; NZ_AQGK01000003.1.
DR AlphaFoldDB; C6XXN8; -.
DR STRING; 485917.Phep_0066; -.
DR KEGG; phe:Phep_0066; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_0_10; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000000852; 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:UP000000852}.
FT DOMAIN 213..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 512 AA; 55977 MW; B839A83FACF5981F CRC64;
MLIKTYGSAV FGVDALTITI EVSIGGGNRY HIVGLPDNAI KESLRRIESA IQSAGLKMPR
QKIVINLAPA DIRKEGSAYD LPIAIAILAA SGQLEIPEVD KYFIMGELSL DGGLQPIKGA
LPISIQARSA GFKGFILPKE NSREAAIVSD IAVYGMCNLM EVVSFFNGSF APHPVLVNTR
DEFLNHINNY EQDFSDVRGQ ENIKRALEIA AAGGHNLILI GPPGAGKTML AKRLPTILPP
LNLHEALETT KIHSVAGKLN AADALMTERP YRSPHHTISD MALVGGGANP QPGEISLAHN
GVLFLDELPE FKRSVLEVMR QPLEDRRVTI SRARLSVEYP ASFMLIASMN PCPCGFFNHP
EKECICAPGQ VQKYLSKISG PLLDRIDLHV EVTPVNFNEL TSAVKAEKSA AIRERVIRAR
AVQDLRFSSR SNLHYNAQMS PNMVREICKI DDAGQTLIKK AMEKLGLSAR AYDRILKVAR
TIADLAASNV ITLEHLAEAI HYRSLDRDSW SG
//
