ID Q6ABM2_CUTAK Unreviewed; 328 AA.
AC Q6ABM2;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=Mg-protoporphyrin IX chelatase {ECO:0000256|ARBA:ARBA00030759};
GN OrderedLocusNames=PPA0100 {ECO:0000313|EMBL:AAT81860.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT81860.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT81860.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family.
CC {ECO:0000256|ARBA:ARBA00005799}.
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DR EMBL; AE017283; AAT81860.1; -; Genomic_DNA.
DR RefSeq; WP_002517368.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6ABM2; -.
DR EnsemblBacteria; AAT81860; AAT81860; PPA0100.
DR KEGG; pac:PPA0100; -.
DR eggNOG; COG1239; Bacteria.
DR HOGENOM; CLU_016684_0_2_11; -.
DR Proteomes; UP000000603; 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; 1.10.8.80; Magnesium chelatase subunit I, C-Terminal domain; 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; IPR041628; ChlI/MoxR_AAA_lid.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR PANTHER; PTHR32039:SF9; MAGNESIUM-CHELATASE SUBUNIT CHLI-1, CHLOROPLASTIC; 1.
DR Pfam; PF17863; AAA_lid_2; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 30..229
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 328 AA; 36121 MW; 2A092F90976D4454 CRC64;
MAQRPVYPFC AIVGQEEMKL ALILATISPD LSGVLIRGEK GTAKSTAVRG LAALLPQHRE
IPGPYHLSPD EYPTHAVALN LPEVMPEPRT VQVPVVELPV GATEDRVTGT LDMETALREG
RRRFEPGLLA AAHRAILYVD EVNLLDDHVV DLLLDSAAMG VNTVEREGVS VTHPARFTLV
GTMNPEEGEL RPQLLDRFGL CVTVSGEDDP DKRTEVIRRR MAFEDDPGGF SRTWEQDGHK
LSERIQRATE LVTQVVISDE TLTTAARTCI NAHVDGHRAD IMMVRAARTL AAWNGCTEIT
TEDLSQAARL VLPHRMRRQP LESVGRAV
//
