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Database: UniProt
Entry: B3ERY7_AMOA5
LinkDB: B3ERY7_AMOA5
Original site: B3ERY7_AMOA5 
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
//
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