ID A0A0E3Y7W9_9ENTR Unreviewed; 420 AA.
AC A0A0E3Y7W9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, 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 ECO:0000313|EMBL:AKC60320.1};
GN ORFNames=BOBLI757_145 {ECO:0000313|EMBL:AKC60320.1};
OS Blochmannia endosymbiont of Camponotus (Colobopsis) obliquus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=1505597 {ECO:0000313|EMBL:AKC60320.1, ECO:0000313|Proteomes:UP000033104};
RN [1] {ECO:0000313|EMBL:AKC60320.1, ECO:0000313|Proteomes:UP000033104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=757 {ECO:0000313|EMBL:AKC60320.1,
RC ECO:0000313|Proteomes:UP000033104};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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; CP010049; AKC60320.1; -; Genomic_DNA.
DR RefSeq; WP_046304639.1; NZ_CP010049.1.
DR AlphaFoldDB; A0A0E3Y7W9; -.
DR STRING; 1505597.BOBLI757_145; -.
DR KEGG; ben:BOBLI757_145; -.
DR PATRIC; fig|1505597.4.peg.141; -.
DR HOGENOM; CLU_037850_3_2_6; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000033104; 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; -; 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:UP000033104}.
FT DOMAIN 10..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 420 AA; 45937 MW; 24C537E8AB287177 CRC64;
MVRVADKRLV VGLEIGTAKV VVLIGEILPD GIVNIIGFGS CPSRGVDKAG VNDLASVVKC
IQQAVNDAEL MADCQITSVY LALSGKHIAC QNEIGIVPIS NEEVTQEDIE NVVHTAKSVR
VCDEHRILHV IPQEYAIDCQ EGIKNPLGLS GIRMQAKVHL ITCHNDMAKN IVKAVERCGL
EVDQLIFAGL ATGYAVLTDD ERELGVCVID IGGGTMDIAI YTDGALRHIK VIPYAGKVVT
SDIAYAFGTP FHEAEIIKIK YGCALYSIVG KEENIEVPSV GGRPPRNLHR QILAEVIEPR
CTELLNLVNN EILQLQKQLH QQGIKHHLAA GVVLTGGSAQ IDGLVICAQK VFNTQVRIGS
PLNISGLIDY VQEPYYSTVV GLLHYGKVSH LNNHLENNKQ TLFGLWLKRI NNWLRKLFFI
//