ID   A0A0W0V7H9_9GAMM        Unreviewed;       535 AA.
AC   A0A0W0V7H9;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acetyl/propionyl-CoA carboxylase, beta subunit {ECO:0000313|EMBL:KTD16042.1};
DE            EC=6.4.1.3 {ECO:0000313|EMBL:KTD16042.1};
GN   ORFNames=Lisr_2189 {ECO:0000313|EMBL:KTD16042.1};
OS   Legionella israelensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=454 {ECO:0000313|EMBL:KTD16042.1, ECO:0000313|Proteomes:UP000054761};
RN   [1] {ECO:0000313|EMBL:KTD16042.1, ECO:0000313|Proteomes:UP000054761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bercovier 4 {ECO:0000313|EMBL:KTD16042.1,
RC   ECO:0000313|Proteomes:UP000054761};
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   -!- 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:KTD16042.1}.
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DR   EMBL; LNYH01000126; KTD16042.1; -; Genomic_DNA.
DR   RefSeq; WP_058502493.1; NZ_UGOE01000001.1.
DR   AlphaFoldDB; A0A0W0V7H9; -.
DR   STRING; 454.Lisr_2189; -.
DR   PATRIC; fig|454.4.peg.2391; -.
DR   OrthoDB; 9803706at2; -.
DR   Proteomes; UP000054761; Unassembled WGS sequence.
DR   GO; GO:0004658; F:propionyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR045190; MCCB/AccD1-like.
DR   PANTHER; PTHR22855; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:KTD16042.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054761}.
FT   DOMAIN          22..278
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          278..523
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   535 AA;  58702 MW;  293A6FBB2500E675 CRC64;
     MAKIISQLNT ESHEFKVNEK AMLKLVNHLQ ESIEKIAQGG DEKARSRHIK HGKRLPRERL
     QYLLDAGSPF LELSQLAAYE VYDAPLPAAG IITGIGRISG TECMIVINDA TVKGGTYYPL
     TVKKHLRAQE IAQINHLPCV YLVDSGGAFL PLQAEVFPDR DHFGRIFFNQ ANMSALNIPQ
     IAVVMGSCTA GGAYVPAMAD ESIMVRNQAT IFLGGPPLVK AATGEVISAE ELGGADVHCR
     ESGVADHYAE NDEHALHLAR VAVSQLNRKK TEFLNRIESR EPAYDIDELN GIIPIDHRKP
     FDMREVIARL VDGSDFDEFK ALFGTTLICG FAHLYGYPVG IIANNGILFG DSALKGAQFI
     QLCCQRRIPL IFLQNITGFM VGSKYEASGI AKHGAKMVMA VANANVPKFT VIVGGSFGAG
     NYAMCGRAYS PRFLWSWPNA RVSVMGGEQA ANVLAQINRD KHQKQGTTWS EDEETSFKDN
     MRNKYETEGN PYYASARLWD DGVIAPRDTR RVLGLSLSAA LNSVSCPTQF GVFRM
//