ID   ACYLL_CAUVN             Reviewed;         572 AA.
AC   A0A0H3C605;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Putative acyl-CoA synthetase CCNA_01223 {ECO:0000303|PubMed:34969973};
DE            EC=6.2.1.- {ECO:0000305};
GN   OrderedLocusNames=CCNA_01223 {ECO:0000312|EMBL:ACL94688.1};
OS   Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=565050;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=20472802; DOI=10.1128/jb.00255-10;
RA   Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA   Walunas T.L., Crosson S.;
RT   "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL   J. Bacteriol. 192:3678-3688(2010).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=33063925; DOI=10.1111/1462-2920.15280;
RA   Olea-Ozuna R.J., Poggio S., Bergstroem E., Quiroz-Rocha E.,
RA   Garcia-Soriano D.A., Sahonero-Canavesi D.X., Padilla-Gomez J.,
RA   Martinez-Aguilar L., Lopez-Lara I.M., Thomas-Oates J., Geiger O.;
RT   "Five structural genes required for ceramide synthesis in Caulobacter and
RT   for bacterial survival.";
RL   Environ. Microbiol. 23:143-159(2021).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NA1000 / CB15N;
RX   PubMed=34969973; DOI=10.1038/s41589-021-00948-7;
RA   Stankeviciute G., Tang P., Ashley B., Chamberlain J.D., Hansen M.E.B.,
RA   Coleman A., D'Emilia R., Fu L., Mohan E.C., Nguyen H., Guan Z.,
RA   Campopiano D.J., Klein E.A.;
RT   "Convergent evolution of bacterial ceramide synthesis.";
RL   Nat. Chem. Biol. 18:305-312(2022).
CC   -!- FUNCTION: Involved in de novo bacterial ceramide synthesis.
CC       {ECO:0000269|PubMed:33063925, ECO:0000269|PubMed:34969973}.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant cannot form bacterial ceramide
CC       (PubMed:33063925, PubMed:34969973). Mutants are impaired in growth at
CC       elevated temperatures but are resistant towards the antibiotic
CC       polymyxin B (PubMed:33063925). {ECO:0000269|PubMed:33063925,
CC       ECO:0000269|PubMed:34969973}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001340; ACL94688.1; -; Genomic_DNA.
DR   RefSeq; WP_012640164.1; NC_011916.1.
DR   RefSeq; YP_002516596.1; NC_011916.1.
DR   EnsemblBacteria; ACL94688; ACL94688; CCNA_01223.
DR   GeneID; 7333616; -.
DR   KEGG; ccs:CCNA_01223; -.
DR   PATRIC; fig|565050.3.peg.1205; -.
DR   HOGENOM; CLU_000022_23_7_5; -.
DR   OMA; NGRNIWP; -.
DR   OrthoDB; 572620at2; -.
DR   PhylomeDB; A0A0H3C605; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000001364; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05931; FAAL; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   Pfam; PF00501; AMP-binding; 1.
PE   3: Inferred from homology;
KW   Ligase; Lipid metabolism; Reference proteome.
FT   CHAIN           1..572
FT                   /note="Putative acyl-CoA synthetase CCNA_01223"
FT                   /id="PRO_0000455456"
SQ   SEQUENCE   572 AA;  61182 MW;  99950691B2A031BF CRC64;
     MKAQLMITPT ASDRTVRFAD FPTLTQALDF AATGETGINL YSLRGELVEA LPYAKLRDEA
     VVLARRLLAI GAKVGDSVAL LAETDGDFVR AFFACQYAGL LPAPMALPTP LGGREAYIEQ
     ISNLARSAKA NILIGPVGLK DWVAEIGARA GLAFAGVLAD LPEDAGAALP TITPEDPCYL
     QFSSGSTRTP TGVLVRHKAL MANCVAITRD GLQVRASDRA ISWLPLYHDM GLIGFLLSPL
     SCQMTVDLLP TGAFVRRPLL WIDLIGRNKA TIAYSPTFGY ELCARRVQGQ SLENYNLSHW
     RSAGLGGDMI RMPPLKAFVE AFAPAGFSDK AFVASYGMAE ATLALSMAPL GKGLRAETLD
     VERLERDALA VDAPEGSERA RDFARCGPAL PDHFLEVRGD DGQVLPERGV GRIFAKGPSV
     MSAYFANPEE TARVLAADGW LDTGDIGFKI DGEIVITGRA KDLIILNGRN IWPQDLEWTA
     DNEIDGLRSG DVCAFAIPAE PEDEVVVLVQ ARGGDADSRA ALRESVATLL RTRHGVEAKV
     KLVGAHALPQ TSSGKLSRSK AKTAYLAGTY GD