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Database: UniProt
Entry: A0A1T4QXJ6_9BACT
LinkDB: A0A1T4QXJ6_9BACT
Original site: A0A1T4QXJ6_9BACT 
ID   A0A1T4QXJ6_9BACT        Unreviewed;       340 AA.
AC   A0A1T4QXJ6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   ORFNames=SAMN04488128_102656 {ECO:0000313|EMBL:SKA08502.1};
OS   Chitinophaga eiseniae.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA08502.1, ECO:0000313|Proteomes:UP000190367};
RN   [1] {ECO:0000313|EMBL:SKA08502.1, ECO:0000313|Proteomes:UP000190367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA08502.1,
RC   ECO:0000313|Proteomes:UP000190367};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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DR   EMBL; FUWZ01000002; SKA08502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4QXJ6; -.
DR   STRING; 634771.SAMN04488128_102656; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000190367; 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; -; 3.
DR   HAMAP; MF_02207; MreB; 1.
DR   InterPro; IPR004000; Actin.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
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   SMART; SM00268; ACTIN; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00329; HSP70_2; 1.
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}.
FT   BINDING         17..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         162..164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         210..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         292..295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   340 AA;  37163 MW;  AE1CD423B339DDF8 CRC64;
     MGFFNFLTQE IAIDLGTANT LIIHNDQVVV DEPSIVAIER ASGKIVAVGK KAMMMHEKTH
     EYLRTIRPLK DGVIADFNAA EGMLRELIKM VYPKKPLFAP SWRMVICIPS SITEVEKRAV
     RDSAEQAGAK EVYLLHEPMA AALGIGIDVE EPVGNMIIDI GGGTTGISVI ALAGIVCDQS
     IRIAGDEFTA DIMEALRRYH SLLIGERTAE QIKIHIGSAL KELDNPPDDI PVNGRDLVTG
     IPKQIMVSYQ EIAEALDKSI FKIEEAILKA LETTPPELAS DIYRRGLYLT GGGALLRGLD
     KRLAQKIKLP VHVADDPLRA VVRGTGIALK HVGKYPFLMQ
//
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