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Entry: A5G8J5_GEOUR
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Original site: A5G8J5_GEOUR 
ID   A5G8J5_GEOUR            Unreviewed;       411 AA.
AC   A5G8J5;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
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   OrderedLocusNames=Gura_3969 {ECO:0000313|EMBL:ABQ28113.1};
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605 {ECO:0000313|EMBL:ABQ28113.1, ECO:0000313|Proteomes:UP000006695};
RN   [1] {ECO:0000313|EMBL:ABQ28113.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rf4 {ECO:0000313|EMBL:ABQ28113.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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 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; CP000698; ABQ28113.1; -; Genomic_DNA.
DR   RefSeq; WP_011940750.1; NC_009483.1.
DR   AlphaFoldDB; A5G8J5; -.
DR   STRING; 351605.Gura_3969; -.
DR   KEGG; gur:Gura_3969; -.
DR   HOGENOM; CLU_037850_3_2_7; -.
DR   OrthoDB; 9810567at2; -.
DR   Proteomes; UP000006695; 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}; 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:UP000006695}.
FT   DOMAIN          9..194
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   411 AA;  43712 MW;  766A80C1B7932050 CRC64;
     MSAKRDNLIV GLDIGTTKIC AIVGNLTEEG IDIVGIGTSP SRGLRKGVVI NIESTVASIR
     KAVEEAELMA GCEIKSVYAG IAGGHIKGFN SQGVIAIKNR EVCSDDVKRV IDAAKAIAIP
     MDREVIHILP QEFIIDDQDG IREPLGMSGV RLEAKVHIVT GAVASAQNII KSCNRAGLDV
     ADIVLEQLAS SEAVLSADEK ELGVALVDVG GGTTDIAIFV DGAIKHTSVL SLGGNHLTND
     IAVGLRTPMA EAEKIKQKYG CCMASLVGKD ETIEVPSVGG RKPRILSRQL LSEILEPRVE
     EIFTLVNREI VKSGLEDLIA SGVVITGGST ILEGMPELAE QVFNLPVRRG LPQRIGGLVD
     VVNSPAYATG VGLVVYGSKN VGVHEFPSAQ SEDNIFRKVS RRMKEWFGEF F
//
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