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Database: UniProt
Entry: A0A0W0XR05_9GAMM
LinkDB: A0A0W0XR05_9GAMM
Original site: A0A0W0XR05_9GAMM 
ID   A0A0W0XR05_9GAMM        Unreviewed;       503 AA.
AC   A0A0W0XR05;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Competence related protein ComM {ECO:0000313|EMBL:KTD47061.1};
GN   Name=comM_1 {ECO:0000313|EMBL:KTD47061.1};
GN   ORFNames=Lrub_1983 {ECO:0000313|EMBL:KTD47061.1};
OS   Legionella rubrilucens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=458 {ECO:0000313|EMBL:KTD47061.1, ECO:0000313|Proteomes:UP000054608};
RN   [1] {ECO:0000313|EMBL:KTD47061.1, ECO:0000313|Proteomes:UP000054608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD47061.1,
RC   ECO:0000313|Proteomes:UP000054608};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTD47061.1}.
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DR   EMBL; LNYT01000020; KTD47061.1; -; Genomic_DNA.
DR   RefSeq; WP_058531976.1; NZ_LNYT01000020.1.
DR   AlphaFoldDB; A0A0W0XR05; -.
DR   STRING; 458.Lrub_1983; -.
DR   PATRIC; fig|458.5.peg.2070; -.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000054608; Unassembled WGS sequence.
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:UP000054608}.
FT   DOMAIN          210..392
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   503 AA;  55146 MW;  3489C34213BF0268 CRC64;
     MNLALTYTRS AQGIHARAVH VEVHLSNGLP QFTIVGLAET AVKESKDRVR SAIINSQFEF
     PCRKITVNLA PADLPKTGSG FDLPIALGIL AASGQIPSEA LASHEFISEL ALSGELRGHT
     PIIPSVVAAR REQRRLIIAE ANAREAALTG YDQVFSAGSL RQVCDYLLHQ TPLDTLPVLP
     PPSAVEPGLD WSDVKGQYHA KQAMVIAACG GHSLLLNGPP GSGKTMLAKR FTTLLPELSE
     TQALECAAIH SLRGKLPPYE HWRIPPFRSP HHTASPVALV GGGSPPKPGE ISLAHHGILF
     LDELPEFHKQ VLETLRQPLE SGLISISRAA MQTDFPAEFQ FIAAMNPCPC GQWGNPRANC
     LCTPDRIKRY LGKLSAPLLD RIDMQVNLQA LSHQELLKAT PTQEGESQRI RLQVQALRAL
     QIRRQGRLNA RLESKACEQV CYLGKEEKAF LSQVLDKLQL SARAYHRFLK VARTIADMKG
     EEQVKRSALQ QALSFKQCLQ MPQ
//
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