ID A0A1M5D7U7_9BACT Unreviewed; 413 AA.
AC A0A1M5D7U7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=SAMN05720760_101102 {ECO:0000313|EMBL:SHF62945.1};
OS Fibrobacter sp. UWB8.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896207 {ECO:0000313|EMBL:SHF62945.1, ECO:0000313|Proteomes:UP000184492};
RN [1] {ECO:0000313|Proteomes:UP000184492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWB8 {ECO:0000313|Proteomes:UP000184492};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FQVZ01000001; SHF62945.1; -; Genomic_DNA.
DR RefSeq; WP_073053426.1; NZ_FQVZ01000001.1.
DR AlphaFoldDB; A0A1M5D7U7; -.
DR Proteomes; UP000184492; 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 14..193
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 413 AA; 44785 MW; 4CE4EB0B7901E593 CRC64;
MDDNKMDKKK DEYIFGLDIG ASKINLFVGV SEGESVRVVE CGDFPLKNAD DLDSVVETLQ
QAVQVIENTT RVDVHDVYVG IAGKHVRSLD TQGLVTLPVG EVREEDIENV TKQASTLPTQ
AGEIIHIFPG EYTLDDEPHI RNPKGLSGRR LKVDVQVVTV RQTALQNLAK CVNRAGLNVA
GFVLEPLAAA SAVLTNDERE LGVALVDIGA GTADIAVFVN DSVRFTYSLE YAGNSITSDI
SCCLNVPIAL SKAEEIKKKY GTCTISNLIE DESFPVPAVG NRGDVSCSRK LLAEIISARV
GEIFKLLSEQ LKAHKLDTII NGGVVLTGGC CALEGIDDVA CRVFGKPARV GRPKGMSGIQ
DAYQNPSYAT GIGLLYYANK QHREKKNRET GTQIAVSVKK GFQRFIEIIR TYL
//
