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Database: UniProt
Entry: Q5L7K0_BACFN
LinkDB: Q5L7K0_BACFN
Original site: Q5L7K0_BACFN 
ID   Q5L7K0_BACFN            Unreviewed;       512 AA.
AC   Q5L7K0; A0A380YUM3;
DT   21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   21-JUN-2005, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=BF9343_4171 {ECO:0000313|EMBL:CAH09952.1};
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09952.1, ECO:0000313|Proteomes:UP000006731};
RN   [1] {ECO:0000313|EMBL:CAH09952.1, ECO:0000313|Proteomes:UP000006731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC   Onslow {ECO:0000313|Proteomes:UP000006731};
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR   EMBL; CR626927; CAH09952.1; -; Genomic_DNA.
DR   RefSeq; WP_010993793.1; NZ_UFTH01000001.1.
DR   PaxDb; 272559-BF9343_4171; -.
DR   KEGG; bfs:BF9343_4171; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_0_10; -.
DR   BioCyc; BFRA272559:G1GHZ-4610-MONOMER; -.
DR   Proteomes; UP000006731; Chromosome.
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:UP000006731}.
FT   DOMAIN          213..396
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   512 AA;  56330 MW;  B741B9E8B3B9341A CRC64;
     MLIKVFGAAV QGIEATLITI EVNSSRGCMF YMVGLPDSAV KESHQRILSA LQVTGYKMPT
     SNIVINMAPA DIRKEGSSYD LPLAIGMLAA GETISCQKLS RYMMMGELSL DGTIQPIKGA
     LPIAIKAREE GFDGLIVPSQ NAREAAVVNN LSVYGVNNIQ EVIEFINGKR ELTPTIVNTR
     EEFYACQSDF EYDFADVKGQ ENVKRALEVA AAGGHNLIMV GAPGSGKSMM AKRLPSILPP
     LSLGESLETT KIHSVAGKLG RNSSLISQRP FRDPHHTISQ VAMVGGGSFP QPGEISLAHN
     GVLFLDELPE FNRSVLEVLR QPLEDRRITI SRVKNTIDYP ASFMLVASMN PCPCGYYNHP
     TKPCVCNPGQ VQKYLNKISG PLLDRIDIQI EIVPVPFEKI SDRQQGESSA TIRQRVIKAR
     QKQEERFSGY PGTYCNAQMT SKQLSSFAQP DTKGLLLLKN AMERLNLSAR AYDRILKVSR
     TIADLEESEQ IQPSHLAEAI SYRNLDRENW AG
//
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