ID A0A0T2KU22_9MICO Unreviewed; 508 AA.
AC A0A0T2KU22;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:KRA23197.1};
GN ORFNames=ASD65_01245 {ECO:0000313|EMBL:KRA23197.1};
OS Microbacterium sp. Root61.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA23197.1, ECO:0000313|Proteomes:UP000051216};
RN [1] {ECO:0000313|EMBL:KRA23197.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA23197.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA23197.1, ECO:0000313|Proteomes:UP000051216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root61 {ECO:0000313|EMBL:KRA23197.1,
RC ECO:0000313|Proteomes:UP000051216};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRA23197.1}.
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DR EMBL; LMGU01000001; KRA23197.1; -; Genomic_DNA.
DR RefSeq; WP_056217345.1; NZ_LMGU01000001.1.
DR AlphaFoldDB; A0A0T2KU22; -.
DR STRING; 1736570.ASD65_01245; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000051216; 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.
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:UP000051216}.
FT DOMAIN 276..351
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 508 AA; 53119 MW; D85BDB48A8F4EF09 CRC64;
MTVARTWAVA LSGIAGELVE VEADLSSQIP EFRLIGLPDK ALGEAVQRVR NACANSDLPL
PRRRLTVNLS PASLPKNGSG FDVAIAIASL ATDVPMDAAS LAATVHIGEL GLDGRLRPVP
GVLPAVLVAL REGKRRAVVP RANLDEAELV DDIEVLGAIS LADVARWHGA DIEAREQAVV
PGPWRPASPS SPLELAEVIG QRDAVEALVV AAAGGHHLLM SGPPGAGKTM LARRLPGILP
PLADDAALAA ASIRSLAGES IDALPRVPPF EAPHHSASVA ALVGGGSRVI RPGAIARASE
GVLFLDEAGE FAAPALDALR QPLETGSITI HRAGATASFP ARFQLVIATN PCPCGNYGVP
GGACICPPQA IRRYLGRLSG PLIDRIDIEL AMTRVSSAHA GAGVTGVSTL VARERVLAAR
DRAARRLRST PWRVNADVSG EWLRHGPYAP PPIARRPLDA ALHRGAITLR GYDRVLRVAW
SISDLDARDA PTVHDIGRAL YLKKGITS
//
