ID A0A0G3H6S5_9CORY Unreviewed; 499 AA.
AC A0A0G3H6S5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Mg chelatase-related protein {ECO:0000313|EMBL:AKK09101.1};
GN ORFNames=CTEST_08355 {ECO:0000313|EMBL:AKK09101.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK09101.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK09101.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK09101.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-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}.
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DR EMBL; CP011545; AKK09101.1; -; Genomic_DNA.
DR RefSeq; WP_047253340.1; NZ_JAASJB010000014.1.
DR AlphaFoldDB; A0A0G3H6S5; -.
DR STRING; 136857.CTEST_08355; -.
DR KEGG; cted:CTEST_08355; -.
DR PATRIC; fig|136857.5.peg.1660; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000035540; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000035540}.
FT DOMAIN 211..389
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 499 AA; 52004 MW; EEA74E7422C998BB CRC64;
MALGRSFTTA LEGVDARIVT VEANIGPGLP GIHVVGLGDA AVSESRDRIR TAFANSQLAW
PKTKIVVSMS PASLRKAGSH FDLPTALAVL AAREPGATAK LDRTIVLGEL GLDGSVREVP
GVLPSLLAAA AHGCEYALIP AASQEQAMLV PGLHVLPVSS LQQAWEWALG ETMLFEASGQ
PTQPAPAPTA DFSDIAGQSE AKLAAEVAAA GGHHLIMIGP PGSGKSMIAA RLPSIMPPLT
PQSCLEATVV HSVVGESGVV TRAPFIAPHH SVSRAALLGG GSGRAHPGAV SLAHHGVLFL
DEVSEIPAAI LDSLRTPLED GEVRLVRSRR EVTFPAQFQL VLAANPCRCA ADDPTRCTCT
SRQRATYLNN LSGPLRDRLD MVINLTGSGA VLTTAFGESS ATIADRVAAA RAKAEQRWSS
HGLAASVNAH VDPHLLRRHH PATEDAMAYL GGLLAQGRIS QRGVDRSLKL SWTLADLAGE
DQPTLDHLGL AVTLRGGRI
//