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Database: UniProt
Entry: A0A1M3ELC5_9CELL
LinkDB: A0A1M3ELC5_9CELL
Original site: A0A1M3ELC5_9CELL 
ID   A0A1M3ELC5_9CELL        Unreviewed;       506 AA.
AC   A0A1M3ELC5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Mg chelatase-like protein {ECO:0000313|EMBL:OJV59566.1};
GN   ORFNames=BGO38_12140 {ECO:0000313|EMBL:OJV59566.1};
OS   Cellulomonas sp. 73-145.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV59566.1, ECO:0000313|Proteomes:UP000184491};
RN   [1] {ECO:0000313|EMBL:OJV59566.1, ECO:0000313|Proteomes:UP000184491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-145 {ECO:0000313|EMBL:OJV59566.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJV59566.1}.
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DR   EMBL; MKTI01000005; OJV59566.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3ELC5; -.
DR   STRING; 1895739.BGO38_12140; -.
DR   Proteomes; UP000184491; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; 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; 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;
FT   DOMAIN          214..398
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   506 AA;  52604 MW;  E1E30EAE81572D88 CRC64;
     MTLGRTRAVS LLGLSGHLVE VEAHLAPSLP AFSLVGLPDT ALAEARDRVR AAVTSSGLVW
     PNRRITVNLS PATLPKAGSG FDLAIAVATL AGAGVVDAAA AADRVHIGEL GLDGRLRPVR
     GVLPAVAAAV AAGHPRVVVP TANAAEASLV PGADVVGAAC LAEVASRYGA DVEVPDLPPV
     HDDVPARRAV VDPDLADVIG QPEARHCLEV AAAGGHHLLM VGPPGAGKTM LAARLPGLLP
     DLAEAEAVEV TAVHSLAGTF DAGDGLVRRP PFEDPHHTAT PASVVGGGSG VPRPGAASRA
     HCGVLFLDEA PEFPTAVLQT LRQPLEHGEV VLHRAAGAAR YPARFQLVLA ANPCPCGRSV
     GKGLECTCRA EQRRRYFGKL SGPLLDRVDL QLEVLPARAE DVPGERSAVV AERVRQARGA
     AVERLAGTGW RTNAQVSGRW LRERLGPRRS LMTDLDRALD RGTLSLRGVD RVLRVAWTLA
     DLQGRAAPSR DDVGRALLLR TRGQGA
//
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