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Database: UniProt
Entry: A0A1Z9JGP0_9CYAN
LinkDB: A0A1Z9JGP0_9CYAN
Original site: A0A1Z9JGP0_9CYAN 
ID   A0A1Z9JGP0_9CYAN        Unreviewed;       510 AA.
AC   A0A1Z9JGP0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=ATP-dependent protease {ECO:0000313|EMBL:OUW29881.1};
GN   ORFNames=CBD37_02430 {ECO:0000313|EMBL:OUW29881.1};
OS   Cyanobacteria bacterium TMED177.
OC   Bacteria; Cyanobacteriota.
OX   NCBI_TaxID=1986677 {ECO:0000313|EMBL:OUW29881.1, ECO:0000313|Proteomes:UP000195337};
RN   [1] {ECO:0000313|EMBL:OUW29881.1, ECO:0000313|Proteomes:UP000195337}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED177 {ECO:0000313|EMBL:OUW29881.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in chlorophyll biosynthesis; introduces a magnesium
CC       ion into protoporphyrin IX to yield Mg-protoporphyrin IX.
CC       {ECO:0000256|ARBA:ARBA00003398}.
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:OUW29881.1}.
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DR   EMBL; NHIA01000019; OUW29881.1; -; Genomic_DNA.
DR   Proteomes; UP000195337; 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   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   Hydrolase {ECO:0000313|EMBL:OUW29881.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000313|EMBL:OUW29881.1}.
FT   DOMAIN          207..391
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   510 AA;  54991 MW;  F365816A43203908 CRC64;
     MLARCLSASL QGLEARPVTV EVDLAPGLPG IQLVGLPDKA IQESRERVRS ALRNAGFRGP
     LVRVVINLAP ADLRKEGPAF DLPIALALLV ASGQLDRPRL NXIWCAGELG LDGSLRPIRG
     VIAIAELAAR HGARALVVPP GNADEAALID GLVVRTAPDL QQLVQQLNGE RPCLRVCRAX
     PEXPPXXHXX IXXQGXAARA LALAAAGGHH LLLVGPPGCG KTHLAHQLPQ LLPPLSREEA
     LTITRIHSXA GQLEQQSPRL LEQRPFRAPH HSCSAAALIG GGVSPQPGXL SLAHGGVLFL
     DELTEFPRAL LDQLRQPLEE GAVRLSRARF KASFPAAITL VAATNPCACG WHGDREHGCR
     CTPSQRQRYW QRLSGPLLDR LDLQLRLERR TAGDVRRCLQ PEDQAREPWL QHEVITAARR
     RMAARNPGGI CNRDLSATAI GEQAGIDNAA WQLWEQLVAR RGLSTRSGIR LLRVARTVAD
     LRGHHGVNAE AVAEASGYRC TDLLLPGSLD
//
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