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Database: UniProt
Entry: A0A379MT30_9BACT
LinkDB: A0A379MT30_9BACT
Original site: A0A379MT30_9BACT 
ID   A0A379MT30_9BACT        Unreviewed;       518 AA.
AC   A0A379MT30;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Competence protein ComM {ECO:0000313|EMBL:SUE34040.1};
GN   Name=comM {ECO:0000313|EMBL:SUE34040.1};
GN   ORFNames=NCTC11190_01257 {ECO:0000313|EMBL:SUE34040.1};
OS   Rikenella microfusus.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Rikenella.
OX   NCBI_TaxID=28139 {ECO:0000313|EMBL:SUE34040.1, ECO:0000313|Proteomes:UP000255233};
RN   [1] {ECO:0000313|EMBL:SUE34040.1, ECO:0000313|Proteomes:UP000255233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11190 {ECO:0000313|EMBL:SUE34040.1,
RC   ECO:0000313|Proteomes:UP000255233};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-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; UGVL01000001; SUE34040.1; -; Genomic_DNA.
DR   RefSeq; WP_027290111.1; NZ_UGVL01000001.1.
DR   AlphaFoldDB; A0A379MT30; -.
DR   STRING; 880526.GCA_000427365_00188; -.
DR   GeneID; 78538192; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000255233; 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   InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
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; PS00676; SIGMA54_INTERACT_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:UP000255233}.
FT   DOMAIN          213..398
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   518 AA;  56822 MW;  07B3F8188E3ACE91 CRC64;
     MLVKTYSSTV EGIDARTITV EVNLSPGIRF LVVGLPDNAV RESQQRITAA FANNRLHMPG
     FNILVNMAPA DMRKVGSHYD LPIAVGILAA SKQVASPMLE RYVLVGELSL DGALLPVKGA
     LPIAVQAWKE GFEGIILPEA NAREAAVVQN LKVYGAADLM QVVALLNGEP VPEPTVIDTR
     AEYFSKLDDF DIDFRDVKGQ GEVKRALEIA AAGGHNVLMI GPPGAGKSML AKRMPTITPP
     MTLAEALETT KIHSVAGKLG DNHSGGLLTA RPFRAPHHIT SEVALVGGGV PPQPGEISLA
     HNGILFLDEL PEFNRRTLEV LRQPLDEKRI TISRAKYSVD YPANFMLIAA MNPCPCGYRT
     HPEKTCTCTP SAQARYMNKI SGPLLDRIDI QVEVIPVAVE SMTRRLREGE TSTQIRERVI
     AARERQTRRL QRDGYANTHN NAMLTPEQME RYCRLDDESI ELIRHAMTTM GLSGRAYDRI
     LKVARTIADL AGSEVIRIDH VAEAIQYRSL DCSHLTNH
//
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