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Database: UniProt
Entry: A0A2S8SUN8_9BACT
LinkDB: A0A2S8SUN8_9BACT
Original site: A0A2S8SUN8_9BACT 
ID   A0A2S8SUN8_9BACT        Unreviewed;       512 AA.
AC   A0A2S8SUN8;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Magnesium chelatase family protein {ECO:0000313|EMBL:PQV64508.1};
GN   ORFNames=B1R32_1041 {ECO:0000313|EMBL:PQV64508.1};
OS   Abditibacterium utsteinense.
OC   Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC   Abditibacteriaceae; Abditibacterium.
OX   NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV64508.1, ECO:0000313|Proteomes:UP000237684};
RN   [1] {ECO:0000313|EMBL:PQV64508.1, ECO:0000313|Proteomes:UP000237684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV64508.1,
RC   ECO:0000313|Proteomes:UP000237684};
RX   PubMed=29475572;
RA   Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT   "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT   candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL   Syst. Appl. Microbiol. 0:0-0(2018).
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:PQV64508.1}.
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DR   EMBL; NIGF01000004; PQV64508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S8SUN8; -.
DR   InParanoid; A0A2S8SUN8; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000237684; 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   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.
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:UP000237684}.
FT   DOMAIN          211..398
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   512 AA;  54838 MW;  F3691370B8F7DE62 CRC64;
     MLAHVDSLAV LGVDAYLVRV EVDVSPGLIS FSVVGLPDAA VRESGERVRA AIRNSGFAMP
     ARRITVNLAP ADTKKQGPIF DLPIALGVLL GDGQIAPRDV KFAACGELGL NGEVRSISGV
     LPMALGARES GKTAILVPKA NAREAAVVEG LEVYAVESLA DAVDWLQNGE KAPVQSDFGL
     ENLEDTPLDL DWADVKGQEA VKRALEVAAA GGHNILLVGA PGSGKTLLSR RLPTILPPLL
     LEEALEVTKL YSVAGLLPAG QSLMSARPFR SPHHTVSHAG LVGGGSFPRP GEISLAHHGV
     LFLDELPEFH RDVLEVMRQP LEDGQVSIAR AAQTLTFPAR FQLVAAMNPC PCGFLLDGGK
     AESKPCTCTA PQIRRYLSRI SGPLLDRIDI HIEVPRLSSE ELMGKRAGES SSCVRKRVVA
     ARKRQTERMR GSGLTCNAQL KAKGLRDYCD MDAGTKDLLK AAIAQFSLSG RGYDRILKVS
     RTIADLEDAQ NIELQHVAEA INYRAFDRKL FG
//
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