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Database: UniProt
Entry: A0A0A3AS56_9PAST
LinkDB: A0A0A3AS56_9PAST
Original site: A0A0A3AS56_9PAST 
ID   A0A0A3AS56_9PAST        Unreviewed;       425 AA.
AC   A0A0A3AS56;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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:KGQ69935.1};
GN   ORFNames=OA57_09940 {ECO:0000313|EMBL:KGQ69935.1};
OS   Chelonobacter oris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Chelonobacter.
OX   NCBI_TaxID=505317 {ECO:0000313|EMBL:KGQ69935.1, ECO:0000313|Proteomes:UP000030380};
RN   [1] {ECO:0000313|EMBL:KGQ69935.1, ECO:0000313|Proteomes:UP000030380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1662 {ECO:0000313|EMBL:KGQ69935.1,
RC   ECO:0000313|Proteomes:UP000030380};
RA   Kudirkiene E., Hansen M.J., Bojesen A.M.;
RT   "Draft genome sequence of Chelonobacter oris 1662T, associated with
RT   respiratory disease in Hermann's Tortoises.";
RL   Submitted (NOV-2014) 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 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGQ69935.1}.
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DR   EMBL; JSUM01000014; KGQ69935.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A3AS56; -.
DR   STRING; 505317.OA57_09940; -.
DR   OrthoDB; 9810567at2; -.
DR   Proteomes; UP000030380; Unassembled WGS sequence.
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};
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:UP000030380}.
FT   DOMAIN          10..196
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   425 AA;  45161 MW;  EB1835A322EBBB83 CRC64;
     MAKIVEAKIK VGLEVGTSKV VAVVGEVLPD GVVNVLGVGS SPSKGIDRGS ITDLDAVVNS
     IQRAIEGAES IADCQIVSVS LAITGEHIQS LNESGLVPIA AGEVTQDEIE GAMNIAQSVK
     MGEGLSILHV IPQEFAVDKQ LNIKNPLGLQ GVRLQAQAHL IACHQSWLNN LKKAVVRAGL
     KVDEVVFSGL ASGYSVLTED EKELGVCLID IGGGTIDIIV YTNGSLRFSK VIPYAGNRVT
     DDVAYAFSTS RMEAEKIKVA HGSAVTPPRN NPDKKIEVPS VGGRAPRSLA KEMLSVVTSA
     RYQELLKLVE KELLVLKHEL EAKQIKSDLI AGIVLTGGGS QIEDIAECAA DIFGPQVRVG
     TPLNLAGLTD YVSKPQYATV LGLLHHNYNN ADEMRQRDAS AGSIGVISGI KENIVKFFTM
     IKNQF
//
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