ID A0A494SSM6_9NOCA Unreviewed; 502 AA.
AC A0A494SSM6;
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:AYJ49416.1};
GN ORFNames=D8W71_15025 {ECO:0000313|EMBL:AYJ49416.1};
OS Rhodococcus sp. P1Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1302308 {ECO:0000313|EMBL:AYJ49416.1, ECO:0000313|Proteomes:UP000277147};
RN [1] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Belimov A., Safronova V.I., Ismailov T.;
RT "Complete genome sequence of the abscisic acid utilizing strain Rhodococcus
RT sp. P1Y.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Nikolaichik Y.A., Gogoleva N.E., Khlopko Y.A., Gogolev Y.V.;
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}.
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DR EMBL; CP032762; AYJ49416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494SSM6; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000277147; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 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 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:0000313|EMBL:AYJ49416.1};
KW Nucleotide-binding {ECO:0000313|EMBL:AYJ49416.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000277147}.
FT DOMAIN 210..392
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 502 AA; 53043 MW; 80F6019EBEA5DFB1 CRC64;
MALGRAFSVA VSGVDGQVVE IEADIGRGLP GTHLVGLPDT ALNESRDRVK AAVTNSGGRW
PDSRVILALS PATLPKMGSV YDLALALSVL DADKQIPRRS LERTVFLGEL ALDGRLRGVR
GVLPGVLAVK RAGWRRVVVP LAALAEAGLV DGIEVLGAVS LSEVVSWLRG EGALDHPVPS
VLVDDAVYPD MSEVVGQSEA RWALEVAAAG AHHIMLTGPP GIGKTMLAQR LPGILPPLTD
EESLEVTAIH SVAGMLTGDR PLISSPPFIA PHHSTTVSAL VGGGTGMAKP GAVSRAHRGV
LFLDECAEMG VKALEALRTP LEDGEIRIAR RDGVARYPAR FQLILAANPC PCAPARNADC
VCAPTVRRKY LGKLSGPLLD RVDIRIAMQT VATGALADEV GETTREVRAR VTGARDAAAE
RWRDFGWRTN AEVPGPALRQ KFRLGNDALR PLERSLRNGS LTARGADRAL RVSWTLADLA
GGDVPGLEEV GAALDFRDRG LM
//