ID A0A0H1AKE3_9GAMM Unreviewed; 503 AA.
AC A0A0H1AKE3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:KLI99312.1};
GN ORFNames=WQ56_13020 {ECO:0000313|EMBL:KLI99312.1};
OS Luteimonas sp. FCS-9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1547516 {ECO:0000313|EMBL:KLI99312.1, ECO:0000313|Proteomes:UP000035397};
RN [1] {ECO:0000313|EMBL:KLI99312.1, ECO:0000313|Proteomes:UP000035397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FCS-9 {ECO:0000313|EMBL:KLI99312.1,
RC ECO:0000313|Proteomes:UP000035397};
RA Bala M., Kumar A., Kaur N., Mathan Kumar R., Kaur G., Singh N.K.,
RA Mayilraj S.;
RT "Taxonomic description and genome sequence of Luteimonas oceanisediminis
RT sp. nov., a novel gammaproteobacteria isolated from a marine sediment.";
RL Submitted (APR-2015) 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:KLI99312.1}.
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DR EMBL; LASZ01000015; KLI99312.1; -; Genomic_DNA.
DR RefSeq; WP_047137554.1; NZ_LASZ01000015.1.
DR AlphaFoldDB; A0A0H1AKE3; -.
DR STRING; 1547516.WQ56_13020; -.
DR PATRIC; fig|1547516.3.peg.2731; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000035397; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
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 Hydrolase {ECO:0000313|EMBL:KLI99312.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:KLI99312.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035397}.
FT DOMAIN 287..382
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
SQ SEQUENCE 503 AA; 52854 MW; 2C2431D58DD0D8C9 CRC64;
MGLALVHGRA RAGIRAPEVQ VEVHLGGGLP SMSIVGLPEA AVREAKDRVR AAIQCAQYEF
PARRITVNLA PADLPKGGGR FDLPIALGIL AASGQVPAEA LRDWEFVGEL GLTGELRAVD
GVLPAALAVA GSGRGLVVPA DNGAEAALAS EVEVRTARTL LEVCALLGGT KPLPVAVAPP
QRTLSGPDMR EVRGQAQARR ALEIAAAGGH HLLLVGPPGC GKTLLASRLP GLLPDAAEAE
ALETAAVLSI SGRGLDPTRW RTRPFRSPHH TASAVALVGG GNEPRPGEIS LAHNGVLFLD
ELPEWDRRAL EVLREPLESG SVTISRAARQ SEFPARFQLV AAMNPCPCGW AGDVSGRCRC
SGEAIARYRA RISGPLLDRI DLHVDVPRLP PTALRPDAPQ GETSAAIRIR VDAARARQHA
RAGTLNARLD QTATALHCRL APADQALLER AIESLHLSAR AMHRILRVAR TIADLDGSPD
IASRHLTEAL GYRGIDTAQP AAA
//
