ID A0A261GHS1_9GAMM Unreviewed; 345 AA.
AC A0A261GHS1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=BTA51_25830 {ECO:0000313|EMBL:OZG70555.1};
OS Hahella sp. CCB-MM4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=1926491 {ECO:0000313|EMBL:OZG70555.1, ECO:0000313|Proteomes:UP000215632};
RN [1] {ECO:0000313|EMBL:OZG70555.1, ECO:0000313|Proteomes:UP000215632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM4 {ECO:0000313|EMBL:OZG70555.1,
RC ECO:0000313|Proteomes:UP000215632};
RA Sam K.-K., Lau N.-S., Dinesh B., Go F., Amirul A.-A.A.;
RT "Genome sequence of Hahella sp. CCB-MM4 and discovery of its potential
RT applications.";
RL Submitted (DEC-2016) 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: 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:OZG70555.1}.
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DR EMBL; MRYI01000021; OZG70555.1; -; Genomic_DNA.
DR RefSeq; WP_020409672.1; NZ_MRYI01000021.1.
DR AlphaFoldDB; A0A261GHS1; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000215632; 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:UP000215632}.
FT BINDING 19..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 166..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 214..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT BINDING 294..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ SEQUENCE 345 AA; 36709 MW; F4AACD9B7F413144 CRC64;
MFKRLRGLFS SDLSIDLGTA NTLIYVRGRG IVLNEPSVVA IRNQGAQKSV AAVGAEAKRM
LGRTPGNITA IRPLKDGVIA DFHVTEKMLQ HFIHKVHENS FITPSPRVLV CIPSRSTQVE
RKAIRESALG AGAREVYLIE EPMAAAIGAG LPVEEASGSM VVDIGGGTTE IAIISLNGIV
NADSVRVGGD KFDEAIATYV RRNYGSLIGD ATAERIKQEI GCAYEGLELR EIDVRGRNLA
EGVPRSFTLN SEEILEALQE ALATIVQAVK SALEQSPPEL ASDIAERGIV LTGGGALLRG
LDNLLTEETG LPVIVADDPL TCVARGGGRA LEVIDKRGSG LFFME
//
