ID A0A1U7DCC8_9RHOB Unreviewed; 443 AA.
AC A0A1U7DCC8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=Ga0080559_TMP4924 {ECO:0000313|EMBL:APX25720.1};
OS Salipiger profundus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1229727 {ECO:0000313|EMBL:APX25720.1, ECO:0000313|Proteomes:UP000186559};
RN [1] {ECO:0000313|EMBL:APX25720.1, ECO:0000313|Proteomes:UP000186559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLT2016 {ECO:0000313|EMBL:APX25720.1,
RC ECO:0000313|Proteomes:UP000186559};
RA Tang K.;
RT "Deep-sea bacteria in the southern Pacific.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014796; APX25720.1; -; Genomic_DNA.
DR RefSeq; WP_076625185.1; NZ_FOLR01000012.1.
DR AlphaFoldDB; A0A1U7DCC8; -.
DR STRING; 1229727.Ga0080559_TMP4924; -.
DR KEGG; tpro:Ga0080559_TMP4924; -.
DR OrthoDB; 9810567at2; -.
DR Proteomes; UP000186559; 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; 3.30.420.40; -; 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:UP000186559}.
FT DOMAIN 24..224
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 443 AA; 47922 MW; 826690F137D686E6 CRC64;
MIELYESQRA MRNMRKAAMQ RGVVAVLDIG SSKIACLVLR FDGTEPITDD GIGSLAGQSG
FRVIGAATTR SRGIKFGEIA AMTETERAIR TAVQAAQKMA NIRVDHVIVS FSGAEPRSYG
LAGQVEVEST MVSEQDVARV LSACDVPDFG SNREVLHAQP VNFALDHRSG LSDPRGQIGQ
ELATDMHMLT VNAQAIQNIA HCMKRCDLEL AGLASSAYAS GISALVEDEQ ELGAACIDMG
GGTTGVSIFM KKHMIYADAV QMGGNHVTGD ISMGLQIPMA MAERIKTFYG GVVATGMDDR
EMIEISGDTG DWHHDRRQVS RAELIGIMRP RVEEILEEVR GCLDAAGFEH MPSQQIVLTG
AASQIPGLDG LASRILGSQV RLGRPMRVHG LPQAATGPGF ASAVGTCLFA AHPQDEWWDF
EIPVDKYPSR SFKRAVKWFR DNW
//
