ID Q057T7_BUCCC Unreviewed; 416 AA.
AC Q057T7;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 77.
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:ABJ90612.1};
GN OrderedLocusNames=BCc_136 {ECO:0000313|EMBL:ABJ90612.1};
OS Buchnera aphidicola subsp. Cinara cedri (strain Cc).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=372461 {ECO:0000313|EMBL:ABJ90612.1, ECO:0000313|Proteomes:UP000000669};
RN [1] {ECO:0000313|EMBL:ABJ90612.1, ECO:0000313|Proteomes:UP000000669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cc {ECO:0000313|Proteomes:UP000000669};
RX PubMed=17038625; DOI=10.1126/science.1130441;
RA Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M.,
RA Silva F.J., Moya A., Latorre A.;
RT "A small microbial genome: the end of a long symbiotic relationship?";
RL Science 314:312-313(2006).
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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02033}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_02033}.
CC Note=Localizes to the Z ring in an FtsZ-dependent manner. Targeted to
CC the membrane through a conserved C-terminal amphipathic helix.
CC {ECO:0000256|HAMAP-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; CP000263; ABJ90612.1; -; Genomic_DNA.
DR RefSeq; WP_011672531.1; NC_008513.1.
DR AlphaFoldDB; Q057T7; -.
DR STRING; 372461.BCc_136; -.
DR KEGG; bcc:BCc_136; -.
DR eggNOG; COG0849; Bacteria.
DR HOGENOM; CLU_037850_3_2_6; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000000669; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000313|EMBL:ABJ90612.1};
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}; Cell inner membrane {ECO:0000256|HAMAP-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 Nucleotide-binding {ECO:0000313|EMBL:ABJ90612.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000669}.
FT DOMAIN 10..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 416 AA; 47263 MW; 047BF2C96D978745 CRC64;
MNLSIKKNII AALEIGTTKI VVLIGEILKN EVINIIGFGK NKSQGIEKGN INNLNLLINC
IKKSIHDAEI MANCKIYTVY LSISHDEINC YNEIGMTPIK KNEITKRDVK KVIKIAKSIK
INNDHKILHM IPQEFSIDKK KGIRNPIGLS GIRMQANVHL ITCNKNISNN IIKAIEKCGI
YVKKNIFVGL ASSLSVLTEE EKNSGVCLVD IGGEVMHVSI FFKGSLYHNA VIPYAGNIVT
RDIAYAFSLS YSDAEFIKKK YGYAVEDIAI ACKNIEIFNK KGIKIKNCHY HSLIEVIEPR
YIELLNLVNN EIIKLYSQYN FKNINNNILK NIIFTGGSSK IKYLLLCAKK IFNTNIEIKK
PCNISEIPKY LSKPEYATII GLLQYGKNYQ KNSFKKKKKN GIFKYFIKNI KYWLTH
//
