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Database: UniProt
Entry: L0W7C5_9GAMM
LinkDB: L0W7C5_9GAMM
Original site: L0W7C5_9GAMM 
ID   L0W7C5_9GAMM            Unreviewed;       496 AA.
AC   L0W7C5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Magnesium chelatase-like protein {ECO:0000313|EMBL:EKF72834.1};
GN   ORFNames=A11A3_16707 {ECO:0000313|EMBL:EKF72834.1};
OS   Alcanivorax hongdengensis A-11-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF72834.1, ECO:0000313|Proteomes:UP000010164};
RN   [1] {ECO:0000313|EMBL:EKF72834.1, ECO:0000313|Proteomes:UP000010164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-11-3 {ECO:0000313|EMBL:EKF72834.1,
RC   ECO:0000313|Proteomes:UP000010164};
RX   PubMed=23209226; DOI=10.1128/JB.01849-12;
RA   Lai Q., Shao Z.;
RT   "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT   hongdengensis Type Strain A-11-3.";
RL   J. Bacteriol. 194:6972-6972(2012).
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:EKF72834.1}.
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DR   EMBL; AMRJ01000049; EKF72834.1; -; Genomic_DNA.
DR   RefSeq; WP_008930506.1; NZ_AMRJ01000049.1.
DR   AlphaFoldDB; L0W7C5; -.
DR   STRING; 1177179.A11A3_16707; -.
DR   PATRIC; fig|1177179.3.peg.3284; -.
DR   eggNOG; COG0606; Bacteria.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000010164; 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          287..382
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   496 AA;  53920 MW;  6D36A34BD6D747C7 CRC64;
     MTHALLHSRV PVGIEARAVR VETHLAPGLP AFSIVGLGDT AVRESRERVR SALVNSGFEF
     PQRRITVSLA PADLPKDGGR FDLPIALGIL LASGQLGRAN TDDYECIGEL ALNGSLSPVP
     GVLPCALACG ESGRTLMVPA DNADEASLAG ATTLAGQRLV DIAAHFTGQA PLTPHDGQMP
     QRRQDDAPCL SDIRGQPQAK RVLEIAAAGG HSLLLSGPPG AGKSMLASRL PGLVPPLGRR
     QALEVAAIHS LRQPRDTDIF YRRPYRAPHH TASASALVGG GSYPRPGEIS LAHHGILFLD
     ELPEFDRKVL EVLREPLETG QVSIARAAQQ LSFPARFQLV AAMNPCPCGY LGDPEKSCGY
     RCEKAKRYQR KLSGPLLDRI DLHLEVPAVE ARELLADREG ETSEQVRERV QRAWQRQWQR
     QQQLNRELRS DALDTLLRPH REWLASAMTR LGLSARALHR SARVARTIAD LADSEAVARD
     HLREALSYRQ SMASTP
//
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