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Database: UniProt
Entry: R7ZSD0_9BACT
LinkDB: R7ZSD0_9BACT
Original site: R7ZSD0_9BACT 
ID   R7ZSD0_9BACT            Unreviewed;       441 AA.
AC   R7ZSD0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=ADIS_2575 {ECO:0000313|EMBL:EON76914.1};
OS   Lunatimonas lonarensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX   NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON76914.1, ECO:0000313|Proteomes:UP000013909};
RN   [1] {ECO:0000313|EMBL:EON76914.1, ECO:0000313|Proteomes:UP000013909}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK24 {ECO:0000313|EMBL:EON76914.1,
RC   ECO:0000313|Proteomes:UP000013909};
RA   Singh A.;
RT   "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL   Submitted (FEB-2013) 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:EON76914.1}.
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DR   EMBL; AQHR01000070; EON76914.1; -; Genomic_DNA.
DR   RefSeq; WP_010854711.1; NZ_AQHR01000070.1.
DR   AlphaFoldDB; R7ZSD0; -.
DR   STRING; 1232681.ADIS_2575; -.
DR   PATRIC; fig|1288963.3.peg.2566; -.
DR   OrthoDB; 9768127at2; -.
DR   Proteomes; UP000013909; 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; -; 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};
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:UP000013909}.
FT   DOMAIN          7..195
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
FT   REGION          392..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  47892 MW;  34469987075A4989 CRC64;
     MENDKLVVGL DIGTTKICAV IGRKNEFGKL EVLGMGKAVS EGVTRGIVTN IDKTTHAIQK
     AVNEASEMSN VDIGEVIVGI AGQHIRSSVH HGVIIRNNQD DEITVEDVRR LANDMENIIV
     PPGNNIIHVM PQDYTVDYED GIKDPVGMSG VRLEADFHII TAQSTAINNI SKCVRRASLI
     SKDLILEPLA SSLSVLSEED REAGVCLVDI GGGTTDVAIF YENIIRHTAV IPFGGNIITT
     DIKEGCMVMQ NQAELLKTKF GKALAEKANP NEIVSIPGLR NRPPKEISVK NLASIIQARM
     EEIIEMVHSE IVASGTYKKL AGGIVLTGGG SLLNGASQLF EYVTGLDTRI GYPNEHLGKS
     KVEEIKSPMY ATTVGLVLAG FKALDDREET YRAKEQNSPM AANARNKTNR LENGPKDIIT
     NITKRLKNFI TDDMGDEAQS Y
//
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