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Database: UniProt
Entry: A0A0A5FYP4_9BACI
LinkDB: A0A0A5FYP4_9BACI
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ID   A0A0A5FYP4_9BACI        Unreviewed;       424 AA.
AC   A0A0A5FYP4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=N783_20570 {ECO:0000313|EMBL:KGX83925.1};
OS   Pontibacillus marinus BH030004 = DSM 16465.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385511 {ECO:0000313|EMBL:KGX83925.1, ECO:0000313|Proteomes:UP000030403};
RN   [1] {ECO:0000313|EMBL:KGX83925.1, ECO:0000313|Proteomes:UP000030403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH030004 {ECO:0000313|EMBL:KGX83925.1,
RC   ECO:0000313|Proteomes:UP000030403};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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   -!- 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:KGX83925.1}.
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DR   EMBL; AVPF01000075; KGX83925.1; -; Genomic_DNA.
DR   RefSeq; WP_027448201.1; NZ_KE384332.1.
DR   AlphaFoldDB; A0A0A5FYP4; -.
DR   STRING; 1385511.GCA_000425225_00953; -.
DR   eggNOG; COG0849; Bacteria.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000030403; 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; 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; PF02491; SHS2_FTSA; 1.
DR   PIRSF; PIRSF003101; FtsA; 1.
DR   SMART; SM00842; FtsA; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
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:UP000030403}.
FT   DOMAIN          7..194
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
FT   REGION          393..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..415
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  46461 MW;  969541592E41C4AE CRC64;
     MNNNDILVSL DIGTSKIKVI IGEVMNDSLN IIGVGTAASN GMKKGAIVDI DQTVQSIRSA
     VEQAERMVGM QINRVVVGIN GNHIQLQPCH GVVAVQSENR EIDEEDINRV LDAAQVMSIP
     PEREIIDVIP QQFIVDGLDE ITDPRGMIGV RLEMEGTIIT CSKTVLHNIL KCVERANLEV
     LDICLQPLAA GSVALSKDEK NLGVALIDIG GGCTTISVFE QGTLQGTSVV PLGGDNITKD
     LSIGMRTSTE EAEDIKRNYG HAFFDEAQED ESFEVSIIGS DRKQSFNQLQ LSDMIEARLE
     EIYAFIEQEI RRMGYRELPG GMVLTGGVVS MPGCLDLAQD VFQSNVRIAI PDYIGVREPQ
     FTSGVGILQF AYHNAKIQGK ELFPAVTIEE PEAKVKKQKK PTTQKEPKKE KESGLSNLIK
     YFFD
//
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