ID K8WWH0_9GAMM Unreviewed; 418 AA.
AC K8WWH0;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
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:EKT64928.1};
GN ORFNames=OOA_01537 {ECO:0000313|EMBL:EKT64928.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT64928.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT64928.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT64928.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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:EKT64928.1}.
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DR EMBL; AKKL01000003; EKT64928.1; -; Genomic_DNA.
DR RefSeq; WP_008910356.1; NZ_KB233222.1.
DR AlphaFoldDB; K8WWH0; -.
DR STRING; 1141662.OOA_01537; -.
DR GeneID; 79872554; -.
DR PATRIC; fig|1141662.3.peg.313; -.
DR eggNOG; COG0849; Bacteria.
DR HOGENOM; CLU_037850_3_2_6; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000009336; 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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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}.
FT DOMAIN 10..196
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 418 AA; 45209 MW; D6C0183FEC4E6EE6 CRC64;
MIKTTDRKLV VGLEIGTSKV SALVGEILPD GMVNIIGVGS CPSRGMDKGG VNDLESVVKC
VQRAIDQAEL MADCQISSVY LALSGKHVSC QNEIGMVPVS EEEVTQEDVD SVVHTAKSVR
VRDEHRILHV IPQEFAIDYQ EGIKNPVGLS GVRMQAKVHL ITCHNDMAKN IVKAVERCGL
KVDQLIFAGL AASYSVLTED ERELGVCVVD IGGGTMDMAV YTGGALRHTK VIPYAGNVVT
SDIAYAFGTP PSDAEAIKVR HGCAVGSIVS KDETVEVPSV GGRPPRSLQR QTLAEVIEPR
YTELLNLVNE EILNLQEQLR QQGVKHHLAA GIVLTGGAAQ IDGLVECAQK VFHTQVRIGT
PLNITGLTDY AQEPYYSTAV GLLHYGKESH LGDDTETEKR ASVKGWFSKI TGWLRKEF
//
