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Database: UniProt
Entry: A5CDY9_ORITB
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Original site: A5CDY9_ORITB 
ID   A5CDY9_ORITB            Unreviewed;       415 AA.
AC   A5CDY9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, 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:CAM80175.1};
GN   OrderedLocusNames=OTBS_1109 {ECO:0000313|EMBL:CAM80175.1};
OS   Orientia tsutsugamushi (strain Boryong) (Rickettsia tsutsugamushi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Orientia.
OX   NCBI_TaxID=357244 {ECO:0000313|EMBL:CAM80175.1, ECO:0000313|Proteomes:UP000001565};
RN   [1] {ECO:0000313|EMBL:CAM80175.1, ECO:0000313|Proteomes:UP000001565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boryong {ECO:0000313|EMBL:CAM80175.1,
RC   ECO:0000313|Proteomes:UP000001565};
RX   PubMed=17483455; DOI=10.1073/pnas.0611553104;
RA   Cho N.-H., Kim H.-R., Lee J.-H., Kim S.-Y., Kim J., Cha S., Kim S.-Y.,
RA   Darby A.C., Fuxelius H.-H., Yin J., Kim J.H., Kim J., Lee S.J., Koh Y.-S.,
RA   Jang W.-J., Park K.-H., Andersson S.G.E., Choi M.-S., Kim I.-S.;
RT   "The Orientia tsutsugamushi genome reveals massive proliferation of
RT   conjugative type IV secretion system and host-cell interaction genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7981-7986(2007).
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; AM494475; CAM80175.1; -; Genomic_DNA.
DR   RefSeq; WP_011944781.1; NC_009488.1.
DR   AlphaFoldDB; A5CDY9; -.
DR   KEGG; ots:OTBS_1109; -.
DR   eggNOG; COG0849; Bacteria.
DR   HOGENOM; CLU_037850_3_0_5; -.
DR   Proteomes; UP000001565; 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   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}; 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   Reference proteome {ECO:0000313|Proteomes:UP000001565}.
FT   DOMAIN          8..194
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   415 AA;  45944 MW;  B584B335D5B035ED CRC64;
     MGTKLSNFVS IDIGSSKIAA VASYVENNGL ISVVSQGFYY SSGIKSGIIS DFKKAENSVI
     SAIYNLEKDL GKTIKHVTIS LSNVCTKSYY TYSKIKIATQ YVTKQDIIKL ISKALYNFKI
     QNQEIIHYFP IEFSLDNNNS IQDPIGMHGK ELGCRLHLIS ANSNVLLNII NCLAKCQVEV
     QEVVLSIYAS GLACLTEDEK NLGAIIIDVG AQTTSFGVFF DGKLLYSGNV AIGGWHITSD
     IAKVLSLSMK TAEKLKVLYG YAMVNMVNKD NIINFEDLDP EANYSNGKSS ITISQLSKII
     QPRAEEILEL VKIEYDKVGV DYLIARCIVL TGGGAILRGF RELVSKIFDK YTRIGIPHLL
     PGLAEDCNSS SYSAVIGVIQ YYANKQHKFY VNANDSDKLK HGLFKQIMLW LRENI
//
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