ID A0A0P7Y854_9RHOB Unreviewed; 504 AA.
AC A0A0P7Y854;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Magnesium chelatase family protein {ECO:0000313|EMBL:KPP84210.1};
GN Name=comM {ECO:0000313|EMBL:KPP84210.1};
GN ORFNames=HLUCCA08_01730 {ECO:0000313|EMBL:KPP84210.1};
OS Rhodobacteraceae bacterium HLUCCA08.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1666913 {ECO:0000313|EMBL:KPP84210.1, ECO:0000313|Proteomes:UP000050293};
RN [1] {ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KPP84210.1, ECO:0000313|Proteomes:UP000050293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLUCCA08 {ECO:0000313|EMBL:KPP84210.1};
RX PubMed=26497460; DOI=10.1128/AEM.02274-15;
RA Nelson W.C., Maezato Y., Wu Y.W., Romine M.F., Lindemann S.R.;
RT "Identification and Resolution of Microdiversity through Metagenomic
RT Sequencing of Parallel Consortia.";
RL Appl. Environ. Microbiol. 82:255-267(2016).
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:KPP84210.1}.
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DR EMBL; LJSF01000043; KPP84210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7Y854; -.
DR STRING; 1666913.HLUCCA08_01730; -.
DR PATRIC; fig|1666913.4.peg.3451; -.
DR Proteomes; UP000050293; 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}.
FT DOMAIN 287..382
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 504 AA; 52828 MW; 53C287E2BD6E8F04 CRC64;
MVAVAYTVAF EGIEARLVEV QCAVSPGLPA FSIVGLPDKA VSEARERVRA ALNAMAIALP
SKRITVNLSP ADMPKEGSHF DLPIALALLA ALEVIPGDAV AQAVALGELS LDGALVSVIG
ALPAAMAAAE EDRILICPRA CGPEAAWVGA TPVYGAGSLA EVLRHFTGQA TITPAEPGEV
TPGPADRDLA DVKGQERARR ALEIAAAGRH HLLMVGSPGS GKSMLAARIP GILPPLTAAE
ALETSMIHSL AGLLDEGGIS RIRPFREPHH TASMAAIVGG GRGAKPGEIS LAHNGVLFMD
EFPEYPRQVL ETLRQPIETG EVVVARANAH VKYPCRFMLV AAANPCKCGY LADPARACAR
VPHCGEDYLG RISGPLMDRF DLRIEVPPVS YTDLDLPGSG EASSAVAARV AAARDRQTTR
FAGAAQMRVN ADAEGAMLEE IATPDAEGRA LLSRVAERFG LSARGYHRIL RVARTIADLD
GAKDVRKPHV AEAVSYRIAA SKEV
//