MREC_CAUVN
ID MREC_CAUVN Reviewed; 346 AA.
AC B8H610;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cell shape-determining protein MreC {ECO:0000250|UniProtKB:P16926};
DE AltName: Full=Cell shape protein MreC {ECO:0000303|PubMed:16344480, ECO:0000303|PubMed:17880425};
DE AltName: Full=Rod shape-determining protein MreC {ECO:0000312|EMBL:ACL95078.1};
GN Name=mreC {ECO:0000312|EMBL:ACL95078.1}; OrderedLocusNames=CCNA_01613;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1] {ECO:0000312|EMBL:ACL95078.1}
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] {ECO:0000305}
RP INTERACTION WITH PENICILLIN-BINDING PROTEINS AND OUTER MEMBRANE PROTEINS,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=NA1000 / CB15N / LS107;
RX PubMed=16344480; DOI=10.1073/pnas.0507937102;
RA Divakaruni A.V., Loo R.R., Xie Y., Loo J.A., Gober J.W.;
RT "The cell-shape protein MreC interacts with extracytoplasmic proteins
RT including cell wall assembly complexes in Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18602-18607(2005).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N / LS107;
RX PubMed=17880425; DOI=10.1111/j.1365-2958.2007.05910.x;
RA Divakaruni A.V., Baida C., White C.L., Gober J.W.;
RT "The cell shape proteins MreB and MreC control cell morphogenesis by
RT positioning cell wall synthetic complexes.";
RL Mol. Microbiol. 66:174-188(2007).
CC -!- FUNCTION: Involved in formation and maintenance of cell shape. Required
CC for the spatial organization of components of the peptidoglycan-
CC synthesizing holoenzyme in the periplasm and peptidoglycan synthetic
CC activity. {ECO:0000250|UniProtKB:P16926, ECO:0000269|PubMed:17880425}.
CC -!- SUBUNIT: Interacts with penicillin-binding proteins (PBP2, PBP1a,
CC PBP1b, PBP2a and PBP2b). Interacts with outer membrane proteins
CC belonging to the TonB-dependent receptor family of transport proteins.
CC {ECO:0000269|PubMed:16344480}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:16344480,
CC ECO:0000269|PubMed:17880425}. Note=Localizes in helical or banded
CC patterns along the cell length. This localization requires a normal
CC cell shape, but is not disrupted in the absence of intracellular
CC filaments formed by MreB. {ECO:0000255, ECO:0000269|PubMed:16344480,
CC ECO:0000269|PubMed:17880425}.
CC -!- DISRUPTION PHENOTYPE: Affects the localization of MltA, MipA and PBP2.
CC In the case of MltA and MipA no polar localization is observed, and in
CC that of PBP2 the banded localization pattern is lost. Depletion of both
CC MreC and RodA results in defects in stalk growth and mutant cells
CC expand relative to wild-type cells. They appear to arrest in expansion
CC along the long axis of the cell. {ECO:0000269|PubMed:17880425}.
CC -!- SIMILARITY: Belongs to the MreC family. {ECO:0000305}.
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DR EMBL; CP001340; ACL95078.1; -; Genomic_DNA.
DR RefSeq; WP_010919418.1; NC_011916.1.
DR RefSeq; YP_002516986.1; NC_011916.1.
DR AlphaFoldDB; B8H610; -.
DR SMR; B8H610; -.
DR PRIDE; B8H610; -.
DR EnsemblBacteria; ACL95078; ACL95078; CCNA_01613.
DR GeneID; 7331591; -.
DR KEGG; ccs:CCNA_01613; -.
DR PATRIC; fig|565050.3.peg.1591; -.
DR HOGENOM; CLU_042663_7_2_5; -.
DR OMA; NPFTHRI; -.
DR OrthoDB; 837894at2; -.
DR PhylomeDB; B8H610; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IDA:UniProtKB.
DR GO; GO:0043164; P:Gram-negative-bacterium-type cell wall biogenesis; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR Gene3D; 2.40.10.340; -; 1.
DR Gene3D; 2.40.10.350; -; 1.
DR InterPro; IPR042177; Cell/Rod_1.
DR InterPro; IPR042175; Cell/Rod_MreC_2.
DR InterPro; IPR007221; MreC.
DR PANTHER; PTHR34138; PTHR34138; 1.
DR Pfam; PF04085; MreC; 1.
PE 1: Evidence at protein level;
KW Cell shape; Coiled coil; Periplasm; Reference proteome.
FT CHAIN 1..346
FT /note="Cell shape-determining protein MreC"
FT /id="PRO_0000418056"
FT REGION 292..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..118
FT /evidence="ECO:0000255"
FT COMPBIAS 292..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 36997 MW; 8F595B357ABF0BA5 CRC64;
MRFREGPLGD LKVPLTWTAA VALIVAAVIG VAFLLADRRE TLQEQAYGVT RQTVDTVARP
VSGAIAAPGR WTGLGLDYVR SYFFTAHENR RLKAELAEMR QWRDRALALQ DQNDRFKSLL
GLRTDPPIPM AAARVVSDSR GPFANTRLAD AGSERGIVVG NPVLNERGLV GRVVGVSRGV
SRVLLLTDIA SRTPVMIDRT NARAILTGDG GPNPKLDYLR GVDPIQQGDR VVTSGDGGVV
PRGLPVGAAV KGLDGRWRVV LFADQASIDY VRILLFKDFA QLADEKQLQA RSLPPVTTED
PQTSILSNPV SRPVAPTPSP ATATPSAAPA ARPATTATPP QTGAPR
