CERS_CAUVN
ID CERS_CAUVN Reviewed; 384 AA.
AC A0A0H3C8X0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Bacterial ceramide synthase {ECO:0000303|PubMed:34969973};
DE EC=2.3.1.- {ECO:0000269|PubMed:34969973};
GN Name=bcerS {ECO:0000303|PubMed:34969973};
GN OrderedLocusNames=CCNA_01212 {ECO:0000312|EMBL:ACL94677.1};
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 (PubMed:33063925, PubMed:34969973). Catalyzes the condensation of 3-
CC oxosphinganine with an acyl-CoA to generate oxidized ceramides
CC (PubMed:34969973). Can use acyl-CoA substrates ranging from C8 to C24,
CC with highest in vitro activity with C14 and very little activity with
CC acyl-CoA thioesters of 18 carbons or longer (PubMed:34969973). May have
CC a preference for monounsaturated acyl-CoA substrates, as it has a
CC threefold greater preference for C16:1-CoA over C16:0-CoA as a
CC substrate in vitro (PubMed:34969973). {ECO:0000269|PubMed:33063925,
CC ECO:0000269|PubMed:34969973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + a fatty acyl-CoA = CoA + H(+) + N-acyl-3-
CC oxosphinganine; Xref=Rhea:RHEA:70359, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58299, ChEBI:CHEBI:77636,
CC ChEBI:CHEBI:189535; Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70360;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + tetradecanoyl-CoA = CoA + H(+) + N-
CC tetradecanoyl-3-oxosphinganine; Xref=Rhea:RHEA:70379,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:58299, ChEBI:CHEBI:189536;
CC Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70380;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + hexadecanoyl-CoA = CoA + H(+) + N-
CC hexadecanoyl-3-oxosphinganine; Xref=Rhea:RHEA:70383,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:58299, ChEBI:CHEBI:189534;
CC Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70384;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 3-oxosphinganine = CoA + H(+) + N-(9Z-
CC hexadecenoyl)-3-oxosphinganine; Xref=Rhea:RHEA:70403,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58299,
CC ChEBI:CHEBI:61540, ChEBI:CHEBI:189544;
CC Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70404;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + octanoyl-CoA = CoA + H(+) + N-octanoyl-3-
CC oxosphinganine; Xref=Rhea:RHEA:70367, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:58299,
CC ChEBI:CHEBI:189539; Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70368;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + decanoyl-CoA = CoA + H(+) + N-decanoyl-3-
CC oxosphinganine; Xref=Rhea:RHEA:70371, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58299, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:189538; Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70372;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + dodecanoyl-CoA = CoA + H(+) + N-dodecanoyl-
CC 3-oxosphinganine; Xref=Rhea:RHEA:70375, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:58299,
CC ChEBI:CHEBI:189537; Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70376;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + octadecanoyl-CoA = CoA + H(+) + N-
CC octadecanoyl-3-oxosphinganine; Xref=Rhea:RHEA:70387,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:58299, ChEBI:CHEBI:189540;
CC Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70388;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + eicosanoyl-CoA = CoA + H(+) + N-eicosanoyl-
CC 3-oxosphinganine; Xref=Rhea:RHEA:70391, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:58299,
CC ChEBI:CHEBI:189541; Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70392;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + docosanoyl-CoA = CoA + H(+) + N-docosanoyl-
CC 3-ketodihydrosphingosine; Xref=Rhea:RHEA:70395, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58299, ChEBI:CHEBI:65059,
CC ChEBI:CHEBI:189542; Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70396;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxosphinganine + tetracosanoyl-CoA = CoA + H(+) + N-
CC tetracosanoyl-3-oxosphinganine; Xref=Rhea:RHEA:70399,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58299,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:189543;
CC Evidence={ECO:0000269|PubMed:34969973};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70400;
CC Evidence={ECO:0000269|PubMed:34969973};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.3 uM for hexadecanoyl-CoA {ECO:0000269|PubMed:34969973};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:34969973}.
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 -!- MISCELLANEOUS: The bacterial ceramide synthesis pathway operates in a
CC different order from that in eukaryotes. Furthermore, phylogenetic
CC analyses support the hypothesis that the bacterial and eukaryotic
CC ceramide pathways evolved independently. {ECO:0000269|PubMed:34969973}.
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DR EMBL; CP001340; ACL94677.1; -; Genomic_DNA.
DR RefSeq; WP_010919038.1; NC_011916.1.
DR RefSeq; YP_002516585.1; NC_011916.1.
DR EnsemblBacteria; ACL94677; ACL94677; CCNA_01212.
DR GeneID; 7333605; -.
DR KEGG; ccs:CCNA_01212; -.
DR PATRIC; fig|565050.3.peg.1194; -.
DR HOGENOM; CLU_053649_0_0_5; -.
DR OMA; AWEKNWG; -.
DR OrthoDB; 884913at2; -.
DR PhylomeDB; A0A0H3C8X0; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR039968; YghO-like.
DR PANTHER; PTHR41368; PTHR41368; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Lipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..384
FT /note="Bacterial ceramide synthase"
FT /id="PRO_0000455453"
SQ SEQUENCE 384 AA; 43279 MW; 8E1C4D83366CF8DF CRC64;
MPFDSTNADL SVIPVKTPAE LKRFIALPAR LNAKDPNWIT PLFMERTDAL TPKTNPFFDH
AEVQLFLATR GGRDVGRISA QIDQLTPQPT EGRLDGHFGM IAAEDDPAVF NVLFRAAEDW
LRARGRTHAV GPFNLSINEE VGLLVWGFDT PPMVLMGHDP VYAGPRVEEQ GYAKAQDLFA
YKADETGDIP EIAQRRVKRG LPSGVVLRQL DMSRYDQEVQ TLTEILNDAW SDNWGFTPTT
EAETRQLAKS LKQVIDQRLV WFSEIDGEAA GVVVFLPNVN EAIADLKGKL LPFGWAKLLW
RLKVKGVKSA RIPLMGVKKK FQTSQRGRML PFWMMKASRD MAMSLGYNRY EISWVLEANK
AMTHIAENVG GTHYKTYRVY EKAL
