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Database: UniProt
Entry: A0A1E3GP61_9GAMM
LinkDB: A0A1E3GP61_9GAMM
Original site: A0A1E3GP61_9GAMM 
ID   A0A1E3GP61_9GAMM        Unreviewed;       500 AA.
AC   A0A1E3GP61;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Competence protein ComM {ECO:0000313|EMBL:ODN65725.1};
GN   Name=comM {ECO:0000313|EMBL:ODN65725.1};
GN   ORFNames=A9E74_02507 {ECO:0000313|EMBL:ODN65725.1};
OS   Methylophaga muralis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN65725.1, ECO:0000313|Proteomes:UP000094379};
RN   [1] {ECO:0000313|EMBL:ODN65725.1, ECO:0000313|Proteomes:UP000094379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bur 1 {ECO:0000313|EMBL:ODN65725.1,
RC   ECO:0000313|Proteomes:UP000094379};
RA   Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA   Mustakhimov I., Trotsenko Y.A.;
RT   "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL   Submitted (JUL-2016) 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:ODN65725.1}.
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DR   EMBL; MCRI01000043; ODN65725.1; -; Genomic_DNA.
DR   RefSeq; WP_069296887.1; NZ_MCRI01000043.1.
DR   AlphaFoldDB; A0A1E3GP61; -.
DR   STRING; 291169.A9E74_02507; -.
DR   PATRIC; fig|291169.3.peg.2529; -.
DR   Proteomes; UP000094379; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094379}.
FT   DOMAIN          209..389
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   500 AA;  54475 MW;  6940248D637456CE CRC64;
     MSIATVYSRA LTGIYAQAVT VEVHLSNGLP SLSIVGMAET AVKESKDRVR SALINSQFTF
     PQQRITINLA PADLPKEGGR FDLPIALGIL AASNQIPVQS LSNMEFIGEL GLTGELRAVR
     GVLPTALATS EANRQLMVPF ENAEEAALTE QGESFAAKTL LEVCSHLHDQ LRLPTNLNKQ
     QHIQNNYADL ADVRGQASAR RALEIAAAGS HSILFAGPPG TGKTMLASRL PGILPPMSEQ
     EAIETATIHS ISSAGFQVEN WMQRPFRAPH HTASAVALVG GGSQPKPGEI SLANHGVLFL
     DELPEFDRKV LEVLREPIES GKITISRAAN QAEFPSKFQL VAAMNPCPCG YLGQARCHCT
     EEQVRRYRGK ISGPLLDRID MLMEVPAVDK KLLRPQPDDV PPESSEVVRQ RVIQARQIQL
     ERANKANASL QHKELEVFCT LSDHDFQLVE KAISRFGLSA RAYHRILKVA RTIADLAGSP
     DIQTVHLTEA IGYRRLDTAN
//
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