GenomeNet

Database: UniProt
Entry: A0A0F0LQ85_9MICO
LinkDB: A0A0F0LQ85_9MICO
Original site: A0A0F0LQ85_9MICO 
ID   A0A0F0LQ85_9MICO        Unreviewed;       512 AA.
AC   A0A0F0LQ85;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Competence protein ComM {ECO:0000313|EMBL:KJL35313.1};
GN   Name=comM {ECO:0000313|EMBL:KJL35313.1};
GN   ORFNames=RR49_02535 {ECO:0000313|EMBL:KJL35313.1};
OS   Microbacterium ginsengisoli.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=400772 {ECO:0000313|EMBL:KJL35313.1, ECO:0000313|Proteomes:UP000033451};
RN   [1] {ECO:0000313|EMBL:KJL35313.1, ECO:0000313|Proteomes:UP000033451}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18659 {ECO:0000313|EMBL:KJL35313.1,
RC   ECO:0000313|Proteomes:UP000033451};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-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:KJL35313.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JYIY01000079; KJL35313.1; -; Genomic_DNA.
DR   RefSeq; WP_045248428.1; NZ_JYIY01000079.1.
DR   AlphaFoldDB; A0A0F0LQ85; -.
DR   STRING; 400772.RR49_02535; -.
DR   PATRIC; fig|400772.4.peg.2547; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000033451; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000033451}.
FT   DOMAIN          220..402
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   512 AA;  53435 MW;  F9E8DB67A8EF2419 CRC64;
     MTVARTAAIA LVGLDGTVVD VEADLTDQQP DLRIIGLGDR ALSEAAQRVT NACMNSGLPL
     PRRRITVNLI PADFPKHGAA FDLAIAVAAL ASAGVLDAAS VARSVHIGEL GLDGRVRAVP
     GVLPAVMAAA RRGCGRVVVP RANLTEAQLV PGIDVVGVAD LRATAVLHGA ELEADDPGDT
     VPTAVSDAAD DDPPVADSAE LADVVGQDAA VEALVVAAAG AHHVLMSGPP GAGKTMLARR
     LPALLPALDD DAALTAAAVA SLSGRRVSRL QRTPPLEAPH HSASVAALVG GGSRTVRPGA
     ISRASGGVLF LDEAGEFPSS VLDALRQPLE RGAIEIHRMG VVAAFPARFQ LVLATNPCPC
     GNHGVRGALC ECPPSAIRRY RARLSGPLLD RIDIEMRMTR VTRVPHSRGR MSSADARERV
     RGARERAARR LRETPWTVNA EIDGAWLRQG PHAPTSDVRA PLDAALERGL LTLRAYDRVL
     RVAWSVADLA GHDRLTGDDI GRALYLKRGM AA
//
DBGET integrated database retrieval system