ID   A0A2R8B2V0_9RHOB        Unreviewed;       504 AA.
AC   A0A2R8B2V0;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Competence protein ComM {ECO:0000313|EMBL:SPH16907.1};
GN   Name=comM {ECO:0000313|EMBL:SPH16907.1};
GN   ORFNames=DEA8626_00421 {ECO:0000313|EMBL:SPH16907.1};
OS   Defluviimonas aquaemixtae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Defluviimonas.
OX   NCBI_TaxID=1542388 {ECO:0000313|EMBL:SPH16907.1, ECO:0000313|Proteomes:UP000244924};
RN   [1] {ECO:0000313|EMBL:SPH16907.1, ECO:0000313|Proteomes:UP000244924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8626 {ECO:0000313|EMBL:SPH16907.1,
RC   ECO:0000313|Proteomes:UP000244924};
RA   Keele B.F.;
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR   EMBL; OMOQ01000001; SPH16907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R8B2V0; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000244924; 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   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: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:UP000244924}.
FT   DOMAIN          208..390
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   504 AA;  53206 MW;  21DC25A857215538 CRC64;
     MVARTYTVAF EGVEARIVEV QCAVSAGMPA FSVVGLPDKA VSEARDRVRA ALTALSIALP
     SKRITVNLSP ADLPKEGSHF DLPIALALLA AIDIIPREDA EATVALGELS LDGRLVPVIG
     ALPAAMAAAE EERTLLCPKA CGPEAAWVEA TPVIAAGSLA EVLGHFTGQA PIAPAQPGEV
     MGARADRDLR DVKGQERAKR ALEIAAAGRH HLLMVGTPGS GKSMLAARMP GILPPLSAVE
     ALETSMIHSL SGLLEEGGIS RTRPFREPHH TASMAAIVGG GRGAKPGEIS LAHNGVLFLD
     ELPEFPRAVL ETLRQPIETG EVVVARANAH IRYPCRFLMV AAANPCKCGY LSEPSRSCAR
     VPQCGEDYLG RISGPLMDRV DLRVEVPPVA YADLDLPDAG EASATVAERV AAARSAQAKR
     FEDHPGVRVN ADAEGRLLED VASPDPEGRD LLAKVAERFG LSARGYHRIL RVARTIADLA
     GSKDVRKPHV AEAVSYRLSV QEGR
//