ID A0A348XPB3_THESC Unreviewed; 414 AA. AC A0A348XPB3; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 05-DEC-2018, entry version 2. 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:HAR68625.1}; GN ORFNames=DCR99_02720 {ECO:0000313|EMBL:HAR68625.1}; OS Thermus scotoductus. OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; OC Thermus. OX NCBI_TaxID=37636 {ECO:0000313|EMBL:HAR68625.1}; RN [1] {ECO:0000313|EMBL:HAR68625.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA10524 {ECO:0000313|EMBL:HAR68625.1}; RX PubMed=30148503; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 0:0-0(2018). CC -!- FUNCTION: Cell division protein that is involved in the assembly CC of the 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: Interacts with FtsZ. {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- CC Rule:MF_02033}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_02033}; Cytoplasmic side {ECO:0000256|HAMAP- CC Rule:MF_02033}. Note=Localizes to the Z ring in an FtsZ-dependent CC manner. Targeted to the membrane through a conserved C-terminal CC amphiphatic helix. {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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HAR68625.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DMVK01000083; HAR68625.1; -; Genomic_DNA. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR HAMAP; MF_02033; FtsA; 1. DR InterPro; IPR020823; Cell_div_FtsA. DR InterPro; IPR003494; SHS2_FtsA. DR Pfam; PF02491; SHS2_FTSA; 1. DR PIRSF; PIRSF003101; FtsA; 1. DR SMART; SM00842; FtsA; 1. DR TIGRFAMs; TIGR01174; ftsA; 1. PE 3: Inferred from homology; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000256|PIRNR:PIRNR003101}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_02033, KW ECO:0000256|PIRNR:PIRNR003101, ECO:0000313|EMBL:HAR68625.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02033}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_02033}. FT DOMAIN 3 190 FtsA. {ECO:0000259|SMART:SM00842}. SQ SEQUENCE 414 AA; 44233 MW; A630A55272E27A4F CRC64; MIIAGLDVGT SKVTTVIGEL APDGVLDIIG EGNVPSQGLK RGVVVNLERT TEAIRQSVHQ AERVAGVKVE RVILGVGGPH LKSVTSHGLA AIRRGQSISA ADVERAIEQA KAYPFDTDLE LLHALPLEFK VDGQEGIRDP VGMAGVRLEV DVHLVAAGRG PLANLRRAVG EAGLEIEALV AQPLASGLGV LSPEEEHMTV LLLDVGGGTT EVAVFREGRL AHSSVLPLGG DHVTQDIAQL LKIPFEEAER VKRKYGAALP ELADPELVLE INQEGGSLGE VPAPELARII RPRLREILHL ARQSVDEALG PLEIKVNRVI LTGGSALLKG FDLLARQQYG LPVRVGKPHG VSGLTDVVAT PAHATAVGLV RYATTLPLTA PEPRRARERR ERREEKAKGE GLWARIKEIL NNLF //