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Database: UniProt
Entry: A0A0L6CS87_9RHOB
LinkDB: A0A0L6CS87_9RHOB
Original site: A0A0L6CS87_9RHOB 
ID   A0A0L6CS87_9RHOB        Unreviewed;       504 AA.
AC   A0A0L6CS87;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Competence protein ComM {ECO:0000313|EMBL:KNX40627.1};
GN   Name=comM {ECO:0000313|EMBL:KNX40627.1};
GN   ORFNames=ROTO_28120 {ECO:0000313|EMBL:KNX40627.1};
OS   Roseovarius tolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX40627.1, ECO:0000313|Proteomes:UP000037046};
RN   [1] {ECO:0000313|Proteomes:UP000037046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA   Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT   "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT   Acylated Alanine Methyl Esters (NAMEs).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNX40627.1}.
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DR   EMBL; LGVV01000045; KNX40627.1; -; Genomic_DNA.
DR   RefSeq; WP_050663663.1; NZ_LGVV01000045.1.
DR   AlphaFoldDB; A0A0L6CS87; -.
DR   STRING; 74031.SAMN04488077_106107; -.
DR   PATRIC; fig|74031.6.peg.2863; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000037046; 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   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.
DR   PROSITE; PS50051; MCM_2; 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:UP000037046}.
FT   DOMAIN          287..382
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   504 AA;  53168 MW;  629C15312EA4C089 CRC64;
     MVARAYTVAF EGVEARTVEV QCAITPGVPA FSLVGLPDKA VSEARDRVRT ALSSMAIALP
     SKRITVNLSP ADLPKEGSHF DLPIALALLA ALEIIPSDAA EGTTALGELS LDGTLIPVIG
     ALPAAMAAAE DNRTLLCPRA CGAEAAWVGA AQVIGAGSLA DVVRHYTGQA PLQPAEAGEV
     IEAAQGRDLR DVKGQERAKR GLEIAAAGRH HLMMVGTPGS GKSMLAARLP GILPPLTAPE
     ALETSMIHSL AGLLSEGGIS RSRPFREPHH TASMAAIVGG GRRASPGEIS LAHNGVLFMD
     EFPEFPRTVL ETLRQPVETG EVMIARANAH VKYPCRFMLV AAANPCKCGY LSDPARACSR
     APNCGEDYMG RISGPLMDRF DLRVEVPPVA FTDLDLPPSG DTSSQVAARV ATARAVQQAR
     FADRPDMRLN ADAEGEALEE IATPDVEGRA LLTRVADRFG LTARGYHRVL RVARTIADLD
     GDKAVRHPHV AEAVSFRIGT LKES
//
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