ID R5FCX0_9BACT Unreviewed; 482 AA.
AC R5FCX0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=BN812_00464 {ECO:0000313|EMBL:CCY02910.1};
OS Prevotella sp. CAG:924.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262938 {ECO:0000313|EMBL:CCY02910.1, ECO:0000313|Proteomes:UP000018357};
RN [1] {ECO:0000313|EMBL:CCY02910.1, ECO:0000313|Proteomes:UP000018357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:924 {ECO:0000313|Proteomes:UP000018357};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY02910.1}.
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DR EMBL; CAXK010000173; CCY02910.1; -; Genomic_DNA.
DR AlphaFoldDB; R5FCX0; -.
DR STRING; 1262938.BN812_00464; -.
DR Proteomes; UP000018357; 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; 3.30.420.40; -; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018357}.
FT DOMAIN 5..191
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 391..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 52792 MW; 641DFE1A74709E87 CRC64;
MADIIVAIEL GSSKITGVAG RKNLDGSINV LSLVSEDSTS CIRKGVVYNI GKTGQALSNI
INKLEQSLKS KIVQVYVGVG GQSIRSVLNS LTKTLPADSV VTQEMVDELM DANRSMDYPE
LKILDAVTQE YRVDQQYQLD PVGIQCAKLE GNYLNILCRR LLYRNLTKCF EQAGITIAEM
YLSPLALADS VLSEAEKRSG CALVDLGADT TTVAVYFKSV LRNLTVIPLG GANITKDIAS
LQMDESEAEA MKLKYASACT DDDDVSSDAK YAIDGDRQVE VMTFNEIVSS RLEEIITNVW
NNVPKEYVGK LIGGVILTGG GSKMKNIEKA FRQLTNVNKV RVAKTVMQTI STSNARVNAK
DGTLCTVLGI LAKGNMNCVG EEINNSLFGG QNTPQAQTGM GTTPSPHVTG QGNGVIKDDP
MKAAEEEARR QREQQEAEEA RLQKEREAEE ERRRRENSGT RKVWRGIKHF FNTMVSPEED
EK
//
