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Database: UniProt
Entry: A0A1A9NE06_9BURK
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Original site: A0A1A9NE06_9BURK 
ID   A0A1A9NE06_9BURK        Unreviewed;       525 AA.
AC   A0A1A9NE06;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Magnesium chelatase {ECO:0000313|EMBL:OAJ64856.1};
GN   ORFNames=A6V37_17595 {ECO:0000313|EMBL:OAJ64856.1};
OS   Paraburkholderia ginsengiterrae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1462993 {ECO:0000313|EMBL:OAJ64856.1, ECO:0000313|Proteomes:UP000078116};
RN   [1] {ECO:0000313|EMBL:OAJ64856.1, ECO:0000313|Proteomes:UP000078116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCY85 {ECO:0000313|EMBL:OAJ64856.1,
RC   ECO:0000313|Proteomes:UP000078116};
RA   Dobritsa A.P., Kutumbaka K., Samadpour M.;
RT   "Reclassification of Paraburkholderia panaciterrae (Farh et al. 2015)
RT   Dobritsa & Samadpour 2016 as a later homotypic synonym of Paraburkholderia
RT   ginsengiterrae (Farh et al. 2015) Dobritsa & Samadpour 2016.";
RL   Submitted (APR-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:OAJ64856.1}.
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DR   EMBL; LXKA01000076; OAJ64856.1; -; Genomic_DNA.
DR   RefSeq; WP_064285846.1; NZ_LXKA01000076.1.
DR   AlphaFoldDB; A0A1A9NE06; -.
DR   STRING; 1462993.A6V36_00490; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000078116; 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.
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          310..407
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   525 AA;  55148 MW;  E08890EAD2FEEA19 CRC64;
     MSLAVVRSRA PASGRAPEVT VEVHLANGLP SFSIVGLPDL EVREGRERVR AALQNCNFDF
     PVRRITVNLA PADLPKESGR FDLPIALGIL AASGQIPAEA LQHREFAGEL SLTGALRPMR
     GAFAMACGTA RSGAAPSSIP DEPLPGETAA HRTPQLYLPA ASAAEAALVP GVDVYGAADL
     PSLCAHLAGA PDARLHPVAA PDLADSAADA VPDMSDVIGQ RGARRALEVA AAGGHHVLLV
     GPPGAGKSML AARLPGLLPA MTDEEALSSA ALLSASRAGF SPSQWRRRPF RAPHHSSSAA
     ALVGGRNPPQ PGEITLAHLG VLFLDELPEF DRDVLETLRE PLEAGRITIS RAALQADFPA
     ACQLIAAMNP CPCGWRGDPN GRCRCTPEIA ARYLRKLSGP LLDRIDIQLE IPALTPAELS
     ARSSASGETS ALIAARVSRA RERQLSRQGK TNRELGGREV DEVCRPDSAG ESLLREAGER
     FGWSARAYYR VLKVARSIAD LAGAAMPSAA QIGEAIQYRR AFGSL
//
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