ID D3SLC1_THEAH Unreviewed; 504 AA.
AC D3SLC1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Mg chelatase, subunit ChlI {ECO:0000313|EMBL:ADC89551.1};
GN OrderedLocusNames=Thal_0919 {ECO:0000313|EMBL:ADC89551.1};
OS Thermocrinis albus (strain DSM 14484 / JCM 11386 / HI 11/12).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Thermocrinis.
OX NCBI_TaxID=638303 {ECO:0000313|EMBL:ADC89551.1, ECO:0000313|Proteomes:UP000002043};
RN [1] {ECO:0000313|Proteomes:UP000002043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14484 / JCM 11386 / HI 11/12
RC {ECO:0000313|Proteomes:UP000002043};
RX DOI=10.4056/sigs.761490;
RA Wirth R., Sikorski J., Brambilla E., Misra M., Lapidus A., Copeland A.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Tapia R., Bruce D., Goodwin L., Pitluck S., Pati A., Anderson I.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Bilek Y., Hader T., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Tindall B.J., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermocrinis albus type strain (HI 11/12T).";
RL Stand. Genomic Sci. 2:194-202(2010).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; CP001931; ADC89551.1; -; Genomic_DNA.
DR RefSeq; WP_012991957.1; NC_013894.1.
DR AlphaFoldDB; D3SLC1; -.
DR STRING; 638303.Thal_0919; -.
DR KEGG; tal:Thal_0919; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_1_0; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000002043; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002043}.
FT DOMAIN 211..392
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 504 AA; 55763 MW; 1BEF4565CF47A314 CRC64;
MFCRVKSGGV WGIEGFEVDV EVDLSPGIPQ FNIVGLPDKA INEAKDRVRS ALRNLGVQLP
AKRITVNLSP SHVRKQGTLY DLPIALGILK LMGTVDLQED TIVLGELSLD GKVRPVSGIL
PIVISLSRLG FRKFLVPSEN ALEGAIVGDV DVYGVSSLEE VVRFLRKEIT LSPQRLHLPS
LMDSFSGYDV DLSEVYGQYQ AKRALEISAA GFHHLLLIGP PGAGKSMLAR RLVTVMPPLS
WEEVLEVTRI YSVAGMLKDP VVLHRPFRAP HYTASEVALI GGGSVPMPGE VSLAHRGVLF
LDEMVEFSRK TLESLRQPLE DGYVTVSRAG GRVTFPAEFL LVGATNPCPC GNYGNPYKKC
VCSPAQIKAY QSRLSGPILD RIDLKVWVQP VEKEDLVSMK KGESSQQVRE RVMKAYAIQQ
ERFRGTPTKY NARMTVDQVR KFCVLTKDAG AFLKEAMDRF RLSARGYMRV LKVARTIADL
AGEELIDTPH IAEALQYRME EFLL
//
