MREB_CAUVN
ID MREB_CAUVN Reviewed; 347 AA.
AC A0A0H3C7V4;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Cell shape-determining protein MreB {ECO:0000255|HAMAP-Rule:MF_02207, ECO:0000305};
DE AltName: Full=Actin-like MreB protein {ECO:0000305};
GN Name=mreB {ECO:0000255|HAMAP-Rule:MF_02207, ECO:0000312|EMBL:ACL95077.1};
GN OrderedLocusNames=CCNA_01612 {ECO:0000312|EMBL:ACL95077.1};
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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N / LS107;
RX PubMed=14982627; DOI=10.1111/j.1365-2958.2003.03936.x;
RA Figge R.M., Divakaruni A.V., Gober J.W.;
RT "MreB, the cell shape-determining bacterial actin homologue, co-ordinates
RT cell wall morphogenesis in Caulobacter crescentus.";
RL Mol. Microbiol. 51:1321-1332(2004).
RN [3]
RP FUNCTION.
RC STRAIN=NA1000 / CB15N;
RX PubMed=15707892; DOI=10.1016/j.cell.2005.01.007;
RA Gitai Z., Dye N.A., Reisenauer A., Wachi M., Shapiro L.;
RT "MreB actin-mediated segregation of a specific region of a bacterial
RT chromosome.";
RL Cell 120:329-341(2005).
RN [4]
RP FUNCTION.
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).
RN [5] {ECO:0007744|PDB:4CZE, ECO:0007744|PDB:4CZF, ECO:0007744|PDB:4CZG, ECO:0007744|PDB:4CZH, ECO:0007744|PDB:4CZI, ECO:0007744|PDB:4CZJ, ECO:0007744|PDB:4CZK, ECO:0007744|PDB:4CZL, ECO:0007744|PDB:4CZM}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 9-347 IN COMPLEXES WITH ADP AND
RP ATP ANALOG, FUNCTION, AND SUBUNIT.
RX PubMed=24843005; DOI=10.7554/elife.02634;
RA van den Ent F., Izore T., Bharat T.A., Johnson C.M., Lowe J.;
RT "Bacterial actin MreB forms antiparallel double filaments.";
RL Elife 3:e02634-e02634(2014).
CC -!- FUNCTION: Forms membrane-associated dynamic filaments that are
CC essential for cell shape determination (PubMed:14982627,
CC PubMed:17880425, PubMed:24843005). Acts by regulating cell wall
CC synthesis and cell elongation, and thus cell shape (PubMed:14982627,
CC PubMed:17880425). A feedback loop between cell geometry and MreB
CC localization may maintain elongated cell shape by targeting cell wall
CC growth to regions of negative cell wall curvature (By similarity).
CC Required for mid-cell peptidoglycan synthesis and cell division.
CC Directs the localization of the cytosolic peptidoglycan precursor-
CC synthesizing enzyme MurG (PubMed:17880425). Also required for proper
CC chromosome segregation (PubMed:15707892). Directs the segregation of
CC origin-proximal but not origin-distal loci (PubMed:15707892).
CC {ECO:0000250|UniProtKB:P0A9X4, ECO:0000269|PubMed:14982627,
CC ECO:0000269|PubMed:15707892, ECO:0000269|PubMed:17880425,
CC ECO:0000269|PubMed:24843005, ECO:0000305|PubMed:14982627}.
CC -!- SUBUNIT: Forms polymers in the presence of ATP. Forms pairs of
CC protofilaments that adopt an antiparallel arrangement and bind to
CC lipids. {ECO:0000269|PubMed:24843005}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14982627}.
CC Note=Membrane-associated (PubMed:14982627). Localizes as bands or
CC spirals that encircled the cell along its entire length and switches to
CC a mid-cell location at a time that coincided with the initiation of
CC cell division. Localization at mid-cell depends on FtsZ
CC (PubMed:14982627). {ECO:0000269|PubMed:14982627}.
CC -!- DISRUPTION PHENOTYPE: Depletion results in lemon-shaped cells that
CC possess defects in the integrity of the cell wall.
CC {ECO:0000269|PubMed:14982627}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000255|HAMAP-
CC Rule:MF_02207, ECO:0000305}.
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DR EMBL; CP001340; ACL95077.1; -; Genomic_DNA.
DR RefSeq; WP_010919417.1; NC_011916.1.
DR RefSeq; YP_002516985.1; NC_011916.1.
DR PDB; 4CZE; X-ray; 2.00 A; A=9-347.
DR PDB; 4CZF; X-ray; 1.64 A; A=9-347.
DR PDB; 4CZG; X-ray; 1.50 A; A=9-347.
DR PDB; 4CZH; X-ray; 1.64 A; A=9-347.
DR PDB; 4CZI; X-ray; 1.80 A; A=9-347.
DR PDB; 4CZJ; X-ray; 2.00 A; A/B=9-347.
DR PDB; 4CZK; X-ray; 2.60 A; A=9-347.
DR PDB; 4CZL; X-ray; 1.60 A; A=9-347.
DR PDB; 4CZM; X-ray; 2.20 A; A/B=9-347.
DR PDBsum; 4CZE; -.
DR PDBsum; 4CZF; -.
DR PDBsum; 4CZG; -.
DR PDBsum; 4CZH; -.
DR PDBsum; 4CZI; -.
DR PDBsum; 4CZJ; -.
DR PDBsum; 4CZK; -.
DR PDBsum; 4CZL; -.
DR PDBsum; 4CZM; -.
DR AlphaFoldDB; A0A0H3C7V4; -.
DR SMR; A0A0H3C7V4; -.
DR EnsemblBacteria; ACL95077; ACL95077; CCNA_01612.
DR GeneID; 7331590; -.
DR KEGG; ccs:CCNA_01612; -.
DR PATRIC; fig|565050.3.peg.1590; -.
DR HOGENOM; CLU_052037_0_0_5; -.
DR OMA; MVICIPS; -.
DR OrthoDB; 410781at2; -.
DR PhylomeDB; A0A0H3C7V4; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd10225; MreB_like; 1.
DR HAMAP; MF_02207; MreB; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004753; MreB.
DR PRINTS; PR01652; SHAPEPROTEIN.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00904; mreB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell shape; Cytoplasm; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..347
FT /note="Cell shape-determining protein MreB"
FT /id="PRO_0000445736"
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207,
FT ECO:0000305|PubMed:24843005"
FT BINDING 165..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207,
FT ECO:0000305|PubMed:24843005"
FT BINDING 213..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207,
FT ECO:0000305|PubMed:24843005"
FT BINDING 295..298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02207,
FT ECO:0000305|PubMed:24843005"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:4CZG"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4CZM"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4CZG"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4CZI"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 188..203
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4CZM"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:4CZG"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 252..275
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:4CZG"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4CZG"
FT HELIX 323..333
FT /evidence="ECO:0007829|PDB:4CZG"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:4CZL"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:4CZL"
SQ SEQUENCE 347 AA; 36685 MW; 4D1C28691CBB9516 CRC64;
MFSSLFGVIS NDIAIDLGTA NTLIYQKGKG IVLNEPSVVA LRNVGGRKVV HAVGIEAKQM
LGRTPGHMEA IRPMRDGVIA DFEVAEEMIK YFIRKVHNRK GFVNPKVIVC VPSGATAVER
RAINDSCLNA GARRVGLIDE PMAAAIGAGL PIHEPTGSMV VDIGGGTTEV AVLSLSGIVY
SRSVRVGGDK MDEAIISYMR RHHNLLIGET TAERIKKEIG TARAPADGEG LSIDVKGRDL
MQGVPREVRI SEKQAADALA EPVGQIVEAV KVALEATPPE LASDIADKGI MLTGGGALLR
GLDAEIRDHT GLPVTVADDP LSCVALGCGK VLEHPKWMKG VLESTLA
