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Database: UniProt
Entry: Q5P700_AROAE
LinkDB: Q5P700_AROAE
Original site: Q5P700_AROAE 
ID   Q5P700_AROAE            Unreviewed;       409 AA.
AC   Q5P700;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 91.
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:CAI06911.1};
GN   ORFNames=ebA1439 {ECO:0000313|EMBL:CAI06911.1};
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06911.1, ECO:0000313|Proteomes:UP000006552};
RN   [1] {ECO:0000313|EMBL:CAI06911.1, ECO:0000313|Proteomes:UP000006552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1 {ECO:0000313|EMBL:CAI06911.1,
RC   ECO:0000313|Proteomes:UP000006552};
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI06911.1; -; Genomic_DNA.
DR   RefSeq; WP_011236639.1; NC_006513.1.
DR   AlphaFoldDB; Q5P700; -.
DR   STRING; 76114.ebA1439; -.
DR   KEGG; eba:ebA1439; -.
DR   eggNOG; COG0849; Bacteria.
DR   HOGENOM; CLU_037850_3_2_4; -.
DR   OrthoDB; 9810567at2; -.
DR   Proteomes; UP000006552; 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; 3.30.420.40; -; 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; 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}; 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:UP000006552}.
FT   DOMAIN          9..195
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   409 AA;  44343 MW;  0B7FBEDF2E26EB56 CRC64;
     MSKEYKDLVV GLDIGTAKVT CMVAESRPDG RLNVIGLATQ PTSGLKRGVV VNIEATVDAI
     ARVIQEVEQM AECKIRDVYT GIAGSHIKSF NSNGMVAIKD KEVTPLDVER VIEVARAMPI
     PAEQQILHIL TQEFIIDGQG GVREPIGMSG VKLEVKVHIV TGAVSAAQNV IKCVRRCGLE
     VMDLILQPLA SSYAVLTEDE KDLGVCLVDI GGGTTDIAVF THGAIRHTAV LPIAGDQVTN
     DIAMALRTPT SEAEEIKIRH GVALHTLADP EEMIEVPGVG DRPPRPLSRQ RLADVIEPRV
     SELFELVQAE LRRSGYEELL SSGVVLTGGS SMMLGMVELG EEVFHMPVRI GSPQYAGGLA
     DVVCQPRYAN AMGLVMEGSA QRRRGMLARE TRSVRQVFGR MKSWFEKNF
//
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