ID B3ERY7_AMOA5 Unreviewed; 512 AA.
AC B3ERY7;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN OrderedLocusNames=Aasi_0588 {ECO:0000313|EMBL:ACE05989.1};
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471 {ECO:0000313|EMBL:ACE05989.1, ECO:0000313|Proteomes:UP000001227};
RN [1] {ECO:0000313|EMBL:ACE05989.1, ECO:0000313|Proteomes:UP000001227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2 {ECO:0000313|EMBL:ACE05989.1,
RC ECO:0000313|Proteomes:UP000001227};
RX PubMed=20023027; DOI=10.1128/JB.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(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; CP001102; ACE05989.1; -; Genomic_DNA.
DR RefSeq; WP_012472755.1; NC_010830.1.
DR AlphaFoldDB; B3ERY7; -.
DR STRING; 452471.Aasi_0588; -.
DR KEGG; aas:Aasi_0588; -.
DR eggNOG; COG0606; Bacteria.
DR HOGENOM; CLU_026145_1_1_10; -.
DR OrthoDB; 9813147at2; -.
DR Proteomes; UP000001227; 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:UP000001227}.
FT DOMAIN 213..396
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 512 AA; 56200 MW; DE89BC165AE7C826 CRC64;
MITSTFGGAV YGVSASLISI EVNIVQGTHL YMVGLPDNAI KESQHRIESV LKHIGCEMPR
QRVIVNLAPA DIRKEGAAYD LPIALCILQA SKQYALRQLG EYVIMGELAL DGTLRSIKGA
LPIAIEARAK KFKGFVLPQE NAHEAAIVNN LDIIPVKNIQ ETLAFFSGSQ HIEPLTIDTR
EIFAEKVQSY ALDFADVQGQ ENIKRALEIA AAGGHNVIMV GPPGAGKTML AKRIPSILPS
FNLHEALETT KVYSVVGKLG KQGTLMTSRP FRSPHHTISD VALVGGGTIP QPGEISLAHN
GVLFLDELPE FKRSVLEVMR QPLEERKVTV ARAKISVDFP ANFMLIASMN PCPCGYYNHP
SKECVCPPSA VQRYLNKVSG PLLDRIDLHI EVTPVPFDEM TAKRKVEDSA AIQARVIEAR
NIQQERFKKH SGIYTNAMMP SAMVKDICCI SKLGQNLLKT AMERLGLSAR AYDRILKVSR
TIADLANSET IGENHLAEAI HYRSLDRQTW GS
//