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Database: UniProt
Entry: A0A1Q3VV95_9PROT
LinkDB: A0A1Q3VV95_9PROT
Original site: A0A1Q3VV95_9PROT 
ID   A0A1Q3VV95_9PROT        Unreviewed;       409 AA.
AC   A0A1Q3VV95;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=BGO63_12110 {ECO:0000313|EMBL:OJW51729.1};
OS   Candidatus Accumulibacter sp. 66-26.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1895689 {ECO:0000313|EMBL:OJW51729.1, ECO:0000313|Proteomes:UP000186203};
RN   [1] {ECO:0000313|EMBL:OJW51729.1, ECO:0000313|Proteomes:UP000186203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=66-26 {ECO:0000313|EMBL:OJW51729.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381}.
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:OJW51729.1}.
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DR   EMBL; MKUH01000008; OJW51729.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3VV95; -.
DR   STRING; 1895689.BGO63_12110; -.
DR   Proteomes; UP000186203; 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; -; 2.
DR   HAMAP; MF_02033; FtsA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR020823; Cell_div_FtsA.
DR   InterPro; IPR018181; Heat_shock_70_CS.
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.
DR   PROSITE; PS01036; HSP70_3; 1.
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          9..195
FT                   /note="SHS2"
FT                   /evidence="ECO:0000259|SMART:SM00842"
SQ   SEQUENCE   409 AA;  44703 MW;  6408CC8491439D8C CRC64;
     MSRDSKDLIV GLDIGTTKIV ALVAEVTPEG RLNVIGMGTQ ESRGLRKGVV VNIEETVAAI
     SRVIQEVELM ADCKVKDVYT GIAGSHIKSF NSNGMVAIKD KEVSTMDLDR VIETARAMPI
     PADQEILHIL TQEFIIDDQD GIREPIGMSG FRLEVKVHIV TGAVSAAQNI VKCVRRCGLE
     VNDLVLQPLA SSYAVLSEDE KDLGICLIDI GGGTTDLAVW TQGAIRHTSV IPIAGDQITN
     DIAMALRTPT REAEEIKRKF GCALSQLADP EDVLDVAGVD DRPSRKLSRR ALADVIQPRV
     EELFELIQAE LRRSGFEEVL SSGIVLTGGS SVMPGMIELG EEIFHMPVRL GIPKYTGALS
     DVVQNPRFST ACGLLLEAQA QRKRGLKVRE TRDFKQVLGR MKSWFEKNF
//
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