ID   A0A077E8J1_9FLAO        Unreviewed;       510 AA.
AC   A0A077E8J1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=MG(2+) CHELATASE FAMILY PROTEIN / ComM-related protein {ECO:0000313|EMBL:AIL43902.1};
GN   ORFNames=BD94_0127 {ECO:0000313|EMBL:AIL43902.1};
OS   Elizabethkingia anophelis NUHP1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Elizabethkingia.
OX   NCBI_TaxID=1338011 {ECO:0000313|EMBL:AIL43902.1, ECO:0000313|Proteomes:UP000028933};
RN   [1] {ECO:0000313|EMBL:AIL43902.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL43902.1};
RX   PubMed=24012265; DOI=10.1016/S0140-6736(13)61858-9;
RA   Teo J., Tan S.Y., Tay M., Ding Y., Kjelleberg S., Givskov M., Lin R.T.,
RA   Yang L.;
RT   "First case of E anophelis outbreak in an intensive-care unit.";
RL   Lancet 382:855-856(2013).
RN   [2] {ECO:0000313|EMBL:AIL43902.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NUHP1 {ECO:0000313|EMBL:AIL43902.1};
RX   PubMed=26019164; DOI=10.1093/gbe/evv101;
RA   Li Y., Liu Y., Chew S.C., Tay M., Salido M.M., Teo J., Lauro F.M.,
RA   Givskov M., Yang L.;
RT   "Complete Genome Sequence and Transcriptomic Analysis of the Novel Pathogen
RT   Elizabethkingia anophelis in Response to Oxidative Stress.";
RL   Genome Biol. Evol. 7:1676-1685(2015).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR   EMBL; CP007547; AIL43902.1; -; Genomic_DNA.
DR   RefSeq; WP_024565394.1; NZ_CP007547.1.
DR   AlphaFoldDB; A0A077E8J1; -.
DR   STRING; 1338011.BD94_0127; -.
DR   KEGG; eao:BD94_0127; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_0_10; -.
DR   Proteomes; UP000028933; 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   CDD; cd00009; AAA; 1.
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   510 AA;  56554 MW;  ED5A42D846C59E8C CRC64;
     MLVKVYGSAI HGISARCITV EVNIDKGVGY YLVGLPDNAI KESSHRISAA LKNVGYKLPG
     RKITINMAPA DLRKEGSAYD LTIAIGILAA NNSIKAENLD KYIIMGELSL DGGLQPLKGI
     LPIALQAAEE GFKGIILPKQ NAQEAAITNN LDVYGVTNIK EVIDFFDQDK PLPKTEFDIQ
     KEFEQKIDRF SSDFSEVKGQ EMAKRALEIA AAGGHNIILI GPPGSGKTML AKRLPGILPP
     LNLKEALETT KIHSVAGKIE NDASLITIRP FRNPHHTISD VALVGGGSYP QPGEISLAHN
     GVLFLDEMPE FKRSVLEVMR QPLEDREVNI SRAKFTVNYP ASFMLVASMN PSPSGYFPDD
     PNNTSSVFEM QRYMNKISGP LLDRIDIHIE VDKVDFEQLS DKKKGETSSE IRQRVIRART
     LQSDRFANLD INYNAQMGPK EIDRFCELNE TSLILLKTAM EKLNLSARAY DRILKVARTI
     ADLENSPYLS SAHISEAIQY RSLDREFWNI
//