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Database: UniProt
Entry: A5UZP9_ROSS1
LinkDB: A5UZP9_ROSS1
Original site: A5UZP9_ROSS1 
ID   A5UZP9_ROSS1            Unreviewed;       505 AA.
AC   A5UZP9;
DT   10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:ABQ92102.1};
GN   OrderedLocusNames=RoseRS_3748 {ECO:0000313|EMBL:ABQ92102.1};
OS   Roseiflexus sp. (strain RS-1).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=357808 {ECO:0000313|EMBL:ABQ92102.1, ECO:0000313|Proteomes:UP000006554};
RN   [1] {ECO:0000313|Proteomes:UP000006554}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-1 {ECO:0000313|Proteomes:UP000006554};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Bryant D.A., Richardson P.;
RT   "Complete sequence of Roseiflexus sp. RS-1.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR   EMBL; CP000686; ABQ92102.1; -; Genomic_DNA.
DR   RefSeq; WP_011958444.1; NC_009523.1.
DR   AlphaFoldDB; A5UZP9; -.
DR   STRING; 357808.RoseRS_3748; -.
DR   KEGG; rrs:RoseRS_3748; -.
DR   eggNOG; COG0606; Bacteria.
DR   HOGENOM; CLU_026145_1_0_0; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000006554; Chromosome.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          211..350
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   505 AA;  54653 MW;  8445611E14AA94C8 CRC64;
     MLAKVYSSAV IGLEGVLVEV EVDIAQGLPA FTIVGLGDTA VQESRERVRA AVRNSGYSFP
     MKRITVNLAP ADLRKAGPAY DLPIAIGLLL ASEQIQGDAS DAVFIGELGL DGAVRHTDGV
     LPMVAVAHER GIRQVFVPKE DAAEASLING VRIVPVERLE DLTAHLSGAR QLPEYTGAPV
     HTELVPEYPV DFSVVRGQEH VKRALEVAAA GGHNVLMTGS PGAGKTLMAR ALISILPPLT
     MSEAIEVTKI YSVAGQLPKD TPLIRQRPFC APHHTTSLAG LVGGGGVRVK PGMVSLAHRG
     VLFLDELPEF GSKLDVLRQP LEDRVVTLSR AVGSITYPAS FMLVAAQNPC VCGWYGDPER
     PCTCTASAVA RYQRRVSGPL LDRFDIFVTV PRVPFEKLNS LQPGEGSTTI RERVIAARQI
     QERRFRGTRA LTNSDMGPAE VHRYCVLDNK SQLVLQSAMR QLDLSARGYH RVLKLARTIA
     DLAGAERITA QHIAEALQYR FHQME
//
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