ID A0A257KI97_9BRAD Unreviewed; 442 AA.
AC A0A257KI97;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|EMBL:OYU86949.1};
GN ORFNames=CFE29_26920 {ECO:0000313|EMBL:OYU86949.1};
OS Bradyrhizobiaceae bacterium PARB1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=2015576 {ECO:0000313|EMBL:OYU86949.1, ECO:0000313|Proteomes:UP000216768};
RN [1] {ECO:0000313|EMBL:OYU86949.1, ECO:0000313|Proteomes:UP000216768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PARB1 {ECO:0000313|EMBL:OYU86949.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU86949.1}.
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DR EMBL; NKIY01000011; OYU86949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257KI97; -.
DR Proteomes; UP000216768; 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 Gene3D; 3.30.1490.110; -; 1.
DR Gene3D; 3.30.420.40; -; 1.
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; 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}.
FT DOMAIN 23..219
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 442 AA; 46653 MW; C7FE1468309FC19B CRC64;
MSGLDRNQAP KTRQMAANRT ALVASLDVGT SKIACMIARL RPCAPNEALR GRTHAVELIG
YSQIQSRGVK SGAVVDMGEA EHSVRQAVGL AERMAKVRVE SVLLSVSAGR LQGQLIEASA
DIKGGAVSAS DMARVTSTGM RHATPPGRTV LHALPVSYSL DGVKGIRDPK GMVASQFGVD
MNVITADATV ARNLMLVVER CHLNVEAMAA APYVAGLSVL TDDETDLGAA VVEMGAGTTT
IATYSGGRIV HASGFAVGGQ HITMDLARGL GCCIADAERI KTLYGTVLTG GSDAREMMNV
PTAGDNDRDY PQAVSRATIA NIVRQRAEEI FEMIRDRLAD SPFAAEPRAR VVLSGGASQL
TGLAELGSQI LGRSVRVARP LGFGRLPMEA KSASFAVPSG LLVYPQFAHL EHVEPRFTRQ
LKTGTDGGGY FGKVGRWLRE GF
//