ID A0A073K378_9BACI Unreviewed; 433 AA.
AC A0A073K378;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Cell division protein FtsA {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101};
GN Name=ftsA {ECO:0000256|HAMAP-Rule:MF_02033};
GN ORFNames=BAMA_08900 {ECO:0000313|EMBL:KEK20902.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK20902.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK20902.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK20902.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cell division protein that is involved in the assembly of the
CC Z ring. May serve as a membrane anchor for the Z ring.
CC {ECO:0000256|HAMAP-Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC -!- SUBUNIT: Self-interacts. Interacts with FtsZ. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_02033};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}. Note=Localizes to
CC the Z ring in an FtsZ-dependent manner. Targeted to the membrane
CC through a conserved C-terminal amphipathic helix. {ECO:0000256|HAMAP-
CC Rule:MF_02033}.
CC -!- SIMILARITY: Belongs to the FtsA/MreB family. {ECO:0000256|HAMAP-
CC Rule:MF_02033, ECO:0000256|PIRNR:PIRNR003101}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381}.
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:KEK20902.1}.
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DR EMBL; JOTN01000002; KEK20902.1; -; Genomic_DNA.
DR RefSeq; WP_034635784.1; NZ_JOTN01000002.1.
DR AlphaFoldDB; A0A073K378; -.
DR STRING; 574376.BAMA_08900; -.
DR eggNOG; COG0849; Bacteria.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000027822; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.1490.110; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_02033; FtsA; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR020823; Cell_div_FtsA.
DR InterPro; IPR021873; FtsA_C.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR003494; SHS2_FtsA.
DR NCBIfam; TIGR01174; ftsA; 1.
DR PANTHER; PTHR32432:SF4; CELL DIVISION PROTEIN FTSA; 1.
DR PANTHER; PTHR32432; CELL DIVISION PROTEIN FTSA-RELATED; 1.
DR Pfam; PF14450; FtsA; 2.
DR Pfam; PF11983; FtsA_C; 1.
DR Pfam; PF02491; SHS2_FTSA; 1.
DR PIRSF; PIRSF003101; FtsA; 1.
DR SMART; SM00842; FtsA; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00329; HSP70_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02033};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02033};
KW Reference proteome {ECO:0000313|Proteomes:UP000027822};
KW Stress response {ECO:0000256|ARBA:ARBA00023016}.
FT DOMAIN 7..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 393..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 433 AA; 47485 MW; 2BE79ECDE69191E9 CRC64;
MNSNEIYVSL DIGTSNVKVI IGEMVNDSLN IIGVGNVKSN GLKKGSIVDI DETVQSIKKA
IEQAERMVGI HIERVVVGVN ANQVQLLPCH GVVAVSNEDR EIGNEDVLRV LDAAQVVSIA
PEREFIDVVP RQFIVDGLDE INDPRGMIGV RLEMEGTLIT GSRTLLHNLL RCVEKAGLEI
VDICLQPLAA ATVALSRDEK NRGVALVDIG GGSTTLSIFQ DGELQATSVL PIGGEHITKD
IAIGLKTSTD SAEQIKVKYG HAFYDTASEE ELFTVPIMGS DQTEQYSQLE LADIIEARVE
EILMFVESEV RRLGVKQLSA GYVLTGGVAS MPGVLDLAYD ILHQNVRIAT PDYIGVREPQ
YTMGVGLIKN ANQKAKLRGK GVQEVQEQYE ELQAPAPVER PVKQKPRTTN NNDNDNNERM
MSKVKRVFRY LWD
//
