ID A0A1G1ZHZ4_9BACT Unreviewed; 409 AA.
AC A0A1G1ZHZ4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 15.
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=A3B92_00030 {ECO:0000313|EMBL:OGY64184.1};
OS Candidatus Harrisonbacteria bacterium RIFCSPHIGHO2_02_FULL_42_16.
OC Bacteria; Candidatus Harrisonbacteria.
OX NCBI_TaxID=1798404 {ECO:0000313|EMBL:OGY64184.1, ECO:0000313|Proteomes:UP000177960};
RN [1] {ECO:0000313|EMBL:OGY64184.1, ECO:0000313|Proteomes:UP000177960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGY64184.1}.
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DR EMBL; MHJG01000008; OGY64184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1ZHZ4; -.
DR STRING; 1798404.A3B92_00030; -.
DR Proteomes; UP000177960; 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; 3.30.420.40; -; 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};
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 6..193
FT /note="SHS2"
FT /evidence="ECO:0000259|SMART:SM00842"
SQ SEQUENCE 409 AA; 43400 MW; 7A8DB9971A962E98 CRC64;
MANNFITGLD IGSQSLKAAV AEVKSDGRTV LVNLFKTPSG GMRKGSVDDL AEMTRSLNIM
FGEIKKVSKN ALKNLFINAN GDVHVQSSRG IVAVSRADNE VYQDDIDRAI QASQAIKLPS
NRMVLHAITK EFVVDGIGDI RDPLGMSGNR LEVNSLIIDA FGPSIKNLTK CVEMAGVSVG
GLIFSPLADS MASLSKNQKD LGVALVDVGF GTTSLCVYEE NKLIHCAVFP VGSGNITNDL
AIGLKTSVEA AEAVKLTYGS ANLKGASGRE QVDLKKIDPD TRSNVSRRFI AEIIEVRLAE
IFEFVNNELK IIGKASQLPV GVVLVGGGCK LSGIVDFVKE EMDLPAQIGI PDIASVESPN
GEISLQAEDP QFVGALGLLM EGRNRMFGDS GGGGGLKNWL KNAINNLLP
//
