ID K0P8T1_9BACT Unreviewed; 512 AA.
AC K0P8T1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Competence protein ComM {ECO:0000313|EMBL:CCM09880.1};
GN Name=comM {ECO:0000313|EMBL:CCM09880.1};
GN ORFNames=CAHE_0098 {ECO:0000313|EMBL:CCM09880.1};
OS Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Cardinium.
OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM09880.1, ECO:0000313|Proteomes:UP000003996};
RN [1] {ECO:0000313|EMBL:CCM09880.1, ECO:0000313|Proteomes:UP000003996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA Malfatti S.A., Hunter M.S., Horn M.;
RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT Incompatibility in Cardinium hertigii.";
RL PLoS Genet. 8:e1003012-e1003012(2012).
CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC subfamily. {ECO:0000256|ARBA:ARBA00006354}.
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DR EMBL; HE983995; CCM09880.1; -; Genomic_DNA.
DR RefSeq; WP_014934254.1; NC_018605.1.
DR AlphaFoldDB; K0P8T1; -.
DR STRING; 1231626.CAHE_0098; -.
DR KEGG; che:CAHE_0098; -.
DR PATRIC; fig|1231626.3.peg.96; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_0_10; -.
DR OrthoDB; 9813147at2; -.
DR BioCyc; CEND1231626:AL022_RS00450-MONOMER; -.
DR Proteomes; UP000003996; 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 213..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 512 AA; 56122 MW; 710DB296853A998E CRC64;
MITRSFSSAV YGVNAFIVSI EVSIVNGTSL FMVGLPDSAI KESQHRIESV LKQIKCTMPR
QRVIVNLAPA DIRKEGASYD LPIALSILHA SEQYNLSRLS AYIIMGELAL DGALRPVKGV
LPIAIEAHKH AFKGMIVPEK NGSEAAVVRK IEVIAVNHIT EAIAFLSGER AIHPIEVDTR
KLFAAQSDAY AVDFADVQGQ ENIKRAFEIA AAGGHNVIMI GPPGAGKTML AKRLPSILPP
FTLAETLETT KVYSIVGRMD SSSGLLSTRP FRAPHHTISD VSLVGGGTFP QPGEISLAHH
GVLFLDELPE FKRSVLEVMR QPLEDGKVVI SRAKFSIEFP ANFMLIASMN PCPCGYYNHP
EKACMCSAVH VQRYLNKVSG PLLDRIDLHV EVVPILFETL TASKKNEASH LIRERVVQAR
QIQQKRFQDH IQLYTNARMS AKLTKLFCPI SVAGQKLLQA AMEKLGLSAR AYERILKVAR
TIADLAGSAN ISEVHLAEAI QYRSLDRAGW GR
//
