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Database: UniProt
Entry: V6Q4U2_9ENTE
LinkDB: V6Q4U2_9ENTE
Original site: V6Q4U2_9ENTE 
ID   V6Q4U2_9ENTE            Unreviewed;       445 AA.
AC   V6Q4U2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=T233_00705 {ECO:0000313|EMBL:EST90139.1};
OS   Vagococcus lutrae LBD1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST90139.1, ECO:0000313|Proteomes:UP000018126};
RN   [1] {ECO:0000313|EMBL:EST90139.1, ECO:0000313|Proteomes:UP000018126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LBD1 {ECO:0000313|EMBL:EST90139.1,
RC   ECO:0000313|Proteomes:UP000018126};
RX   PubMed=24371201;
RA   Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA   Earl A.M., Gilmore M.S.;
RT   "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT   Isolated from the Largemouth Bass Micropterus salmoides.";
RL   Genome Announc. 1:e01087-13(2013).
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:EST90139.1}.
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DR   EMBL; AYSH01000010; EST90139.1; -; Genomic_DNA.
DR   RefSeq; WP_023606037.1; NZ_AYSH01000010.1.
DR   AlphaFoldDB; V6Q4U2; -.
DR   STRING; 1408226.T233_00705; -.
DR   PATRIC; fig|1408226.3.peg.678; -.
DR   eggNOG; COG0849; Bacteria.
DR   Proteomes; UP000018126; 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; 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; 1.
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.
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:UP000018126}.
FT   DOMAIN          7..194
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   445 AA;  48223 MW;  8B118426E8A48164 CRC64;
     MANTGIHVGL DIGTTSVKVV VAEYIEGQIN IIGVGNAKSE GLNRGIVIDI DKAANTIKRA
     IAQAEEKSGV QIRKVNVGLP ANLLEIEPCE GMIAVSAESK EITDEDVQNV ASAAIVRSTP
     PERQVITLIP REYKVDGFDG IKDPRGMLGV RLDMQGLVFT GPKTIIHNVK KCVEKAGLEL
     GELVITPLAL AETVLTDGEK DFGTTLIDMG GGQTTAAVYY DNQLQFTHVE QEGGEFVTKD
     ISVVLNTSIH NAEALKINYG DAYTERTSED EVFPVEVIGK PEPIKVDERY LSEIIEARME
     QIFTKVKHSL VNTDALNLPG GVIITGGNAG MPGVTELASE ILGTNVHLHV PNHMGLRNPI
     FSNAISIVEY VATLSDIYRI SQFAVTGERF AQTASSTMPR VQFQEPTEVE MTHYEEPVAN
     VSDAPKGTNE KLSDKIKGFF SNMFD
//
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