ID Q2GEX7_NEOSM Unreviewed; 501 AA.
AC Q2GEX7;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Mg chelatase-related protein {ECO:0000313|EMBL:ABD46508.1};
GN OrderedLocusNames=NSE_0068 {ECO:0000313|EMBL:ABD46508.1};
OS Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS sennetsu).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Neorickettsia.
OX NCBI_TaxID=222891 {ECO:0000313|EMBL:ABD46508.1, ECO:0000313|Proteomes:UP000001942};
RN [1] {ECO:0000313|EMBL:ABD46508.1, ECO:0000313|Proteomes:UP000001942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-367 / Miyayama {ECO:0000313|Proteomes:UP000001942};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP000237; ABD46508.1; -; Genomic_DNA.
DR RefSeq; WP_011451475.1; NC_007798.1.
DR AlphaFoldDB; Q2GEX7; -.
DR STRING; 222891.NSE_0068; -.
DR KEGG; nse:NSE_0068; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_1_5; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000001942; 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}.
FT DOMAIN 209..388
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 501 AA; 55583 MW; E8BF947A41B2E50D CRC64;
MFTEIHTISI QGLSLVKIGV QVAISPGLPC FNIVGLPDKS ISESKERIRA ALLHIGLSLP
KKRITVNLSP AGLTKIGTHY DLPIALGVIQ LLDSNFVNRN FSEFVVLGEL SLDASVKGVA
GVLPAAIYAK ERNLWLVCPW ENRIEARISK NKKLLPIASL NELTSFLMGK STPKKICDTF
VLEEDSYPDM KDVKGQKIAK RAIEIAAAGG HHMLMRGPPG TGKSMLAKRI VGIMPPLLPK
EIMEVNTIIS VSGEFTNKIY RKRPFREPHQ SASAAAMIGG GAVPKPGEVT LAHNGVLFLD
EMAEFSSHVL DTLRQVLETG EVTISRANMK LTYPASFQLI GAMNPCRCGY LGYLPEKECK
NSKKCGLEYM KTISGPFLDR IDIFVNMEPI NKNQFFESQD GESSALIRKR VIAARNKQYE
RYNKVKFSLN CHMDNHALAE HVSLDNETRE FLKATFEKGY ISLRGHDRIL KVARTIADLD
GSDEVKKAHL TEALYYRMSQ N
//