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Database: UniProt
Entry: A0A3S4Z5R2_9NEIS
LinkDB: A0A3S4Z5R2_9NEIS
Original site: A0A3S4Z5R2_9NEIS 
ID   A0A3S4Z5R2_9NEIS        Unreviewed;       346 AA.
AC   A0A3S4Z5R2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Cell shape-determining protein MreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   Name=hscA_1 {ECO:0000313|EMBL:VEJ49163.1};
GN   Synonyms=mreB {ECO:0000256|HAMAP-Rule:MF_02207};
GN   ORFNames=NCTC12742_00060 {ECO:0000313|EMBL:VEJ49163.1};
OS   Neisseria weaveri.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=28091 {ECO:0000313|EMBL:VEJ49163.1, ECO:0000313|Proteomes:UP000272771};
RN   [1] {ECO:0000313|EMBL:VEJ49163.1, ECO:0000313|Proteomes:UP000272771}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12742 {ECO:0000313|EMBL:VEJ49163.1,
RC   ECO:0000313|Proteomes:UP000272771};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) 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}.
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DR   EMBL; LR134533; VEJ49163.1; -; Genomic_DNA.
DR   RefSeq; WP_004284707.1; NZ_POXU01000005.1.
DR   AlphaFoldDB; A0A3S4Z5R2; -.
DR   STRING; 28091.SAMEA3174300_00716; -.
DR   KEGG; nwe:SAMEA3174300_0716; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000272771; Chromosome 1.
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; 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:UP000272771}.
FT   BINDING         19..21
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         167..169
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         215..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
FT   BINDING         295..298
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02207"
SQ   SEQUENCE   346 AA;  36637 MW;  1D22DB1F55D2D8B6 CRC64;
     MFRFLTRYFS NDLAIDLGTA NTLIYIRNKG IVLDEPSVVA MQNDVAHGKS VILAVGTEAK
     KMLGRTPGSI QAIRPMKDGV IADFNVTEKM LKQFIKKVNN SRFAAAPRIV ICVPCGSTQV
     ERKAIRDSAL AAGASTVNLI EEPMAAAIGA GLPIEEATGS MVVDIGGGTT EVGVISLSGV
     VYSHSIRVGG DAFDDSIINY VRRNYGMLIG EATAEEIKKN IGSAFPGMEV KEIEVKGRNL
     AEGIPRSFTI SSNEVLEALT EPLNQIVQSV KNALEQTPPE LGADIAERGL VLTGGGALLK
     GLDRLLAEET GLPVMIAEDP LTCVARGSGK ALDMIGKLNS VFVVNP
//
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