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Database: UniProt
Entry: A0A1V4IPV1_9CLOT
LinkDB: A0A1V4IPV1_9CLOT
Original site: A0A1V4IPV1_9CLOT 
ID   A0A1V4IPV1_9CLOT        Unreviewed;       338 AA.
AC   A0A1V4IPV1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=mreB_2 {ECO:0000313|EMBL:OPJ62042.1};
GN   Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   ORFNames=CLCHR_21780 {ECO:0000313|EMBL:OPJ62042.1}, D2A34_22965
GN   {ECO:0000313|EMBL:RII32532.1}, GKZ28_16295
GN   {ECO:0000313|EMBL:MVX65253.1};
OS   Clostridium chromiireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ62042.1, ECO:0000313|Proteomes:UP000191056};
RN   [1] {ECO:0000313|EMBL:OPJ62042.1, ECO:0000313|Proteomes:UP000191056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ62042.1,
RC   ECO:0000313|Proteomes:UP000191056};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RII32532.1, ECO:0000313|Proteomes:UP000265930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C1 {ECO:0000313|EMBL:RII32532.1,
RC   ECO:0000313|Proteomes:UP000265930};
RA   Xing M., Wei Y., Ang E.L., Zhao H., Zhang Y.;
RT   "Genome of Clostridium chromiireducens C1, DSM12136.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:MVX65253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NM79_F5 {ECO:0000313|EMBL:MVX65253.1};
RA   Navarre W., Wong E.;
RT   "Microbes associate with the intestines of laboratory mice.";
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms membrane-associated dynamic filaments that are
CC       essential for cell shape determination. Acts by regulating cell wall
CC       synthesis and cell elongation, and thus cell shape. A feedback loop
CC       between cell geometry and MreB localization may maintain elongated cell
CC       shape by targeting cell wall growth to regions of negative cell wall
CC       curvature. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC   -!- SUBUNIT: Forms polymers. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02207}.
CC       Note=Membrane-associated. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC   -!- SIMILARITY: Belongs to the FtsA/MreB family.
CC       {ECO:0000256|ARBA:ARBA00023458, ECO:0000256|HAMAP-Rule:MF_02207}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_02207}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ62042.1}.
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DR   EMBL; WSRQ01000028; MVX65253.1; -; Genomic_DNA.
DR   EMBL; MZGT01000026; OPJ62042.1; -; Genomic_DNA.
DR   EMBL; QXDJ01000007; RII32532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4IPV1; -.
DR   STRING; 225345.CLCHR_21780; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000191056; Unassembled WGS sequence.
DR   Proteomes; UP000265930; Unassembled WGS sequence.
DR   Proteomes; UP000656077; Unassembled WGS sequence.
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   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_02207; MreB; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004753; MreB.
DR   NCBIfam; TIGR00904; mreB; 1.
DR   PANTHER; PTHR42749; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR   PANTHER; PTHR42749:SF1; CELL SHAPE-DETERMINING PROTEIN MREB; 1.
DR   Pfam; PF06723; MreB_Mbl; 1.
DR   PRINTS; PR01652; SHAPEPROTEIN.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_02207};
KW   Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW   Rule:MF_02207}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02207};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02207};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191056}.
FT   BINDING         16..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         160..162
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         208..211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   338 AA;  36179 MW;  7AF503DDCF4545B8 CRC64;
     MGFFGSGKDM GIDLGTANTL VFVKGKGIVL REPSVVAMNT MTKKTLAVGS EAKLMIGRTP
     GNIVAIRPLK DGVIADFDTA QTMMKSLIEK VSTKNAFKNP RIIVCYPSGV TEVEKRAIEE
     ATKLSGARDV ILMEEPMAAA IGAGLPVSEP TGSMIVDIGG GTTEVAIISL GGIVTSKSLR
     IAGDELDQSI ISYIKKEFNL MVGERTAEQV KMEIGSAYRT SEEEMVMEIK GRDMITGLPK
     IVEISETQVR EALKEPVYAI IESIKTTLEK TPPELAADIM EKGIMLAGGG AYLRGLDVLI
     NKETNMPVHI AEAPLDCVVL GAGKALEDFD KISRDQRG
//
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