ID A0A494XEP0_9BURK Unreviewed; 539 AA.
AC A0A494XEP0;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=ATP-binding protein {ECO:0000313|EMBL:RKP49257.1};
GN ORFNames=D7S89_10790 {ECO:0000313|EMBL:RKP49257.1};
OS Trinickia fusca.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2419777 {ECO:0000313|EMBL:RKP49257.1, ECO:0000313|Proteomes:UP000280434};
RN [1] {ECO:0000313|EMBL:RKP49257.1, ECO:0000313|Proteomes:UP000280434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7MK8-2 {ECO:0000313|EMBL:RKP49257.1,
RC ECO:0000313|Proteomes:UP000280434};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. 7MK8-2, isolated from soil.";
RL Submitted (OCT-2018) 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:RKP49257.1}.
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DR EMBL; RBZV01000003; RKP49257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XEP0; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000280434; 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, ECO:0000313|EMBL:RKP49257.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000280434}.
FT DOMAIN 326..386
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 539 AA; 57679 MW; 578B235801678952 CRC64;
MSLAVVRSRA PAAGRAPEVT VEVHLANGLP SFSIVGLPDL EVRESRERVR AALQNCGFDF
PVRRITVNLA PADLPKESGR FDLPIALGIL AASGQLPAAS LGEREFAGEL SLTGALRPMR
GAFAMACGMA RGRLRVPARA ADSADDTEFK RDASAEVRES TTELMRTRTP ELYLPLASAG
EAALVPGVCV YGAADLPSLC AHLAGTPECR LRPITAPSLE QVVPAEHPDM ADVIGQRGAR
RALEVAAAGG HHMLMVGPPG AGKSMLAARL PGLLPPMSDE DALTSAALLS ASRVGFSPGQ
WRRRPFRAPH HSSSAAALVG GRNPPQPGEI TLAHLGVLFL DELPEFDRHV LETLREPLEA
GRITISRAAL QADFPAACQL VAAMNPCPCG WRGDPAGRCR CTPEVAARYL RKLSGPLLDR
IDIQIELPAL TPAELSARAS EPAEPSAAIA LRVARARERQ LVRQRKMNRE LTGREIDDMC
PLGPEAELLL REASDRFGWS ARAYYRVLKV ARTIADLAGP DVPDAAHVAE AIQYRRVFT
//