ID A0A0U2YZ13_9BACL Unreviewed; 429 AA.
AC A0A0U2YZ13;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AUC31_17015 {ECO:0000313|EMBL:ALS76814.1};
OS Planococcus rifietoensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=200991 {ECO:0000313|EMBL:ALS76814.1, ECO:0000313|Proteomes:UP000067683};
RN [1] {ECO:0000313|EMBL:ALS76814.1, ECO:0000313|Proteomes:UP000067683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:ALS76814.1,
RC ECO:0000313|Proteomes:UP000067683};
RA See-Too W.S.;
RT "Complete genome of Planococcus rifietoensis type strain M8.";
RL Submitted (JAN-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; CP013659; ALS76814.1; -; Genomic_DNA.
DR RefSeq; WP_058383515.1; NZ_CP013659.2.
DR AlphaFoldDB; A0A0U2YZ13; -.
DR STRING; 200991.AUC31_17015; -.
DR KEGG; prt:AUC31_17015; -.
DR OrthoDB; 9768127at2; -.
DR Proteomes; UP000067683; Chromosome.
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:UP000067683}.
FT DOMAIN 7..194
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
FT REGION 384..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 47234 MW; 5E3479B1B7BE3421 CRC64;
MSQSELYVSL DIGSSSVKVL IGEMTNKSLH VIGVGNVKSN GIKKGAIVDI DATVQSIKKA
VDQAERMIGK EIHEVVLGIP ANQVALQPVK GIVAVNSENR EITDEDLERV LEAAQVMSIP
PERELVNIIP EEYVVDHLGE IKDPRGMIGI RLEMDGTMVT TSKTVLHNVL RCVERAGLEI
REIYVQPLVA GSYALTEDEK NHGTACIDIG GGSTSIAVFR DGHLRAASVI PVGGDHVTKD
LSIVLKTPTE QAEKIKLEHG HAFFDDASEE EVFEVPVIGS DSREQYSQKY ISEIIGVRME
ELFELILDEL YRLGVDELPG GVVLTGGMAK MDGLPELARS ILQTRVRLFT PEFIGVREPQ
YTTAVGLIQY AYAEDLFYGN VGHSSAATHS QKPEYVEQQP KKQKQPKQPK QDNEGVVSKA
KKMFDRFFE
//
