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Database: UniProt
Entry: C7JH85_ACEP3
LinkDB: C7JH85_ACEP3
Original site: C7JH85_ACEP3 
ID   C7JH85_ACEP3            Unreviewed;       503 AA.
AC   C7JH85;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Magnesium chelatase-related protein {ECO:0000313|EMBL:BAH99339.1};
GN   OrderedLocusNames=APA01_11920 {ECO:0000313|EMBL:BAH99339.1};
OS   Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH99339.1, ECO:0000313|Proteomes:UP000000948};
RN   [1] {ECO:0000313|EMBL:BAH99339.1, ECO:0000313|Proteomes:UP000000948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX   PubMed=19638423; DOI=10.1093/nar/gkp612;
RA   Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA   Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT   "Whole-genome analyses reveal genetic instability of Acetobacter
RT   pasteurianus.";
RL   Nucleic Acids Res. 37:5768-5783(2009).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR   EMBL; AP011121; BAH99339.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7JH85; -.
DR   STRING; 634452.APA01_11920; -.
DR   KEGG; apt:APA01_11920; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_1_5; -.
DR   BioCyc; APAS634452:APA01_RS06025-MONOMER; -.
DR   Proteomes; UP000000948; Chromosome.
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   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          295..390
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   503 AA;  53289 MW;  FE0EFC134A939FB3 CRC64;
     MSIGAGILNS RIRSFAFCGI EARPVWVEVQ ISSGLPAFLM VGLPDKAVAE ARERVRAALT
     SIGLALPAKR ILVNLVPADI PKEGSHFDLP IALALLTAMG VIPGEEVARY AALGELSLDG
     RLNPVAGVLS ASLEAASMNL GLVCPAAQGQ EALCGGDISI LAAPDLLALI NHFNGLQVLS
     PPEFSAQEDE PVSEPDLADI RGMETGRRAL EIAAAGGHSL LLSGPPGAGK SMLAARLPSL
     LPDLLVAESL DVSRIYSAAG LLVGGRPIRR PPFRDPHHSA SLPALVGGGA RARPGEISLA
     HRGVLFLDEL PEFSRSALEA LRQPLETGQI SIARAAVHVT YPARFQLIAA MNPCRCGYLG
     DASRECRKAP RCGEDYMNRL SGPLLDRIDM HLAMQPYEPL GYMAGPPGEN SATVAERVRC
     ARQMQAERQG ARKNAEAALE DLCVSVEAQN MAQAIAARFR FSARGYTRML RVARSIADLA
     GELDIQPQHV AEAATYRSRG SAN
//
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