LARC_LACPL
ID LARC_LACPL Reviewed; 420 AA.
AC F9UST1; F9UST2;
DT 27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Pyridinium-3,5-bisthiocarboxylic acid mononucleotide nickel insertion protein {ECO:0000305|PubMed:27114550};
DE Short=P2TMN nickel insertion protein {ECO:0000305|PubMed:27114550};
DE EC=4.99.1.12 {ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:27114550};
DE AltName: Full=Lactate racemase accessory protein LarC {ECO:0000303|PubMed:24710389};
DE AltName: Full=Lactate racemase activation protein LarC {ECO:0000303|PubMed:24710389};
DE AltName: Full=Lactate racemase maturation protein LarC {ECO:0000303|PubMed:24710389};
DE AltName: Full=Lactate racemization operon protein LarC {ECO:0000303|PubMed:24710389};
DE AltName: Full=Nickel-pincer cofactor biosynthesis protein LarC {ECO:0000305|PubMed:27114550};
GN Name=larC {ECO:0000303|PubMed:24710389};
GN Synonyms=larC1/larC2 {ECO:0000312|EMBL:CCC77662.1,
GN ECO:0000312|EMBL:CCC77663.1};
GN OrderedLocusNames=lp_0106/lp_0107 {ECO:0000312|EMBL:CCC77662.1,
GN ECO:0000312|EMBL:CCC77663.1};
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=16166538; DOI=10.1128/jb.187.19.6750-6761.2005;
RA Goffin P., Deghorain M., Mainardi J.L., Tytgat I., Champomier-Verges M.C.,
RA Kleerebezem M., Hols P.;
RT "Lactate racemization as a rescue pathway for supplying D-lactate to the
RT cell wall biosynthesis machinery in Lactobacillus plantarum.";
RL J. Bacteriol. 187:6750-6761(2005).
RN [4]
RP RIBOSOMAL FRAMESHIFT, FUNCTION, CATALYTIC ACTIVITY, NICKEL-BINDING,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=24710389; DOI=10.1038/ncomms4615;
RA Desguin B., Goffin P., Viaene E., Kleerebezem M., Martin-Diaconescu V.,
RA Maroney M.J., Declercq J.P., Soumillion P., Hols P.;
RT "Lactate racemase is a nickel-dependent enzyme activated by a widespread
RT maturation system.";
RL Nat. Commun. 5:3615-3615(2014).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27114550; DOI=10.1073/pnas.1600486113;
RA Desguin B., Soumillion P., Hols P., Hausinger R.P.;
RT "Nickel-pincer cofactor biosynthesis involves LarB-catalyzed pyridinium
RT carboxylation and LarE-dependent sacrificial sulfur insertion.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:5598-5603(2016).
CC -!- FUNCTION: Involved in the biosynthesis of a nickel-pincer cofactor
CC ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel
CC delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide
CC (P2TMN), to form the mature cofactor. Is required for the activation of
CC the lactate racemase LarA. May also be involved in the activation of
CC other nickel-pincer cofactor-dependent enzymes.
CC {ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:27114550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide =
CC Ni(2+) + pyridinium-3,5-bisthiocarboxylate mononucleotide;
CC Xref=Rhea:RHEA:54784, ChEBI:CHEBI:49786, ChEBI:CHEBI:137372,
CC ChEBI:CHEBI:137373; EC=4.99.1.12;
CC Evidence={ECO:0000269|PubMed:24710389, ECO:0000269|PubMed:27114550};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Ribosomal frameshifting; Named isoforms=2;
CC Name=1;
CC IsoId=F9UST1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F9UST1-2; Sequence=VSP_059080;
CC -!- INDUCTION: Induced by L-lactate and repressed by D-lactate. Is thus
CC regulated by the L-lactate/D-lactate ratio. Makes part of the lar
CC operon (larABCDE). {ECO:0000269|PubMed:16166538,
CC ECO:0000269|PubMed:24710389}.
CC -!- DISRUPTION PHENOTYPE: Deletion of this gene leads to a loss of lactate
CC racemase activity. {ECO:0000269|PubMed:24710389}.
CC -!- MISCELLANEOUS: [Isoform 1]: Expression of the full-length LarC protein
CC requires a -1 ribosomal frameshift to allow contiguous translation of
CC larC1 and larC2 ORFs, leading to the functional form of the protein.
CC The exact position of the frameshift cannot be determined but likely
CC occurs in the stretch of 10 consecutive adenines present at the end of
CC larC1. {ECO:0000269|PubMed:24710389}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced from conventional translation of
CC the larC1 ORF. Expression of LarC1 alone does not show lactate racemase
CC activity. {ECO:0000269|PubMed:24710389}.
CC -!- SIMILARITY: Belongs to the LarC family. {ECO:0000255|HAMAP-
CC Rule:MF_01074}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCC77662.1; Type=Frameshift; Note=The exact position of the ribosomal frameshift cannot be determined but likely occurs in the 10 consecutive adenines present at the end of larC1.; Evidence={ECO:0000269|PubMed:24710389};
CC Sequence=CCC77663.1; Type=Frameshift; Evidence={ECO:0000269|PubMed:24710389};
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; AL935263; CCC77662.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL935263; CCC77663.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; YP_004888176.1; NC_004567.2.
DR RefSeq; YP_004888177.1; NC_004567.2.
DR PDB; 6BWO; X-ray; 2.03 A; A/B=272-420.
DR PDB; 6BWQ; X-ray; 1.85 A; A/B=272-420.
DR PDB; 6BWR; X-ray; 1.81 A; A/B=272-420.
DR PDBsum; 6BWO; -.
DR PDBsum; 6BWQ; -.
DR PDBsum; 6BWR; -.
DR AlphaFoldDB; F9UST1; -.
DR SMR; F9UST1; -.
DR STRING; 220668.lp_0106; -.
DR EnsemblBacteria; CCC77662; CCC77662; lp_0106.
DR EnsemblBacteria; CCC77663; CCC77663; lp_0107.
DR KEGG; lpl:lp_0106; -.
DR KEGG; lpl:lp_0107; -.
DR eggNOG; COG1641; Bacteria.
DR HOGENOM; CLU_028523_1_0_9; -.
DR OMA; DMFIGAL; -.
DR PhylomeDB; F9UST1; -.
DR BioCyc; LPLA220668:G1GW0-84-MON; -.
DR BioCyc; MetaCyc:MON-20307; -.
DR BRENDA; 4.99.1.12; 2849.
DR Proteomes; UP000000432; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051604; P:protein maturation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01074; LarC; 1.
DR InterPro; IPR002822; Ni_insertion.
DR PANTHER; PTHR36566; PTHR36566; 1.
DR Pfam; PF01969; DUF111; 1.
DR TIGRFAMs; TIGR00299; TIGR00299; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Nickel; Reference proteome; Ribosomal frameshifting.
FT CHAIN 1..420
FT /note="Pyridinium-3,5-bisthiocarboxylic acid mononucleotide
FT nickel insertion protein"
FT /id="PRO_0000441654"
FT VAR_SEQ 263..420
FT /note="KLSQQIVNRTADAVLMIEANLDDQTGEGLGYVMNQLLTAGAYDVFFTPIQMK
FT KDRPATKLTVLGNVNDKDLLTKLILQETTTIGVRYQTWQRTIMQRHFLTVATPYGDVQV
FT KVATYQDIEKKMPEYADCAQLAQQFHIPFRTVYQAALVAVDQLDEEA -> N (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_059080"
FT STRAND 273..285
FT /evidence="ECO:0007829|PDB:6BWR"
FT HELIX 288..300
FT /evidence="ECO:0007829|PDB:6BWR"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:6BWR"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6BWR"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:6BWR"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6BWR"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:6BWR"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:6BWR"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:6BWR"
FT STRAND 369..378
FT /evidence="ECO:0007829|PDB:6BWR"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:6BWR"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:6BWR"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:6BWR"
SQ SEQUENCE 420 AA; 46391 MW; ABDD9A1F1486C404 CRC64;
MQTLYLDAFS GISGDMFLGA LLDLGLDFEQ LKTELAKLHV HGYELTQQRE AQSSIYGTSF
DVQVAGGKDH GFVEHHHHQH EAGHHHDHEA RHLADIEALI DGSDLSDTVK HHAKAIFMEI
AQAEAAVHHM PLAEVHFHEV GALDSIVDIV GCCIGLELMQ IDTIMASPLS DGSGFINVAH
GQMPVPVPAV MQMRVGSAIP IQQRLDVHTE LITPTGMGLV KTLVREFGPL PENAVPTRVG
YGFGKRDTGG FNALRAVLFE KKKLSQQIVN RTADAVLMIE ANLDDQTGEG LGYVMNQLLT
AGAYDVFFTP IQMKKDRPAT KLTVLGNVND KDLLTKLILQ ETTTIGVRYQ TWQRTIMQRH
FLTVATPYGD VQVKVATYQD IEKKMPEYAD CAQLAQQFHI PFRTVYQAAL VAVDQLDEEA
