FZLA_CAUVN
ID FZLA_CAUVN Reviewed; 228 AA.
AC A0A0H3CDY2;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=FtsZ-localized protein A {ECO:0000303|PubMed:20864042};
DE AltName: Full=FtsZ-binding protein FzlA {ECO:0000305};
GN Name=fzlA {ECO:0000303|PubMed:20864042};
GN OrderedLocusNames=CCNA_03754 {ECO:0000312|EMBL:ACL97219.2};
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP FUNCTION, INTERACTION WITH FTSZ, SUBCELLULAR LOCATION, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=20864042; DOI=10.1016/j.molcel.2010.08.027;
RA Goley E.D., Dye N.A., Werner J.N., Gitai Z., Shapiro L.;
RT "Imaging-based identification of a critical regulator of FtsZ protofilament
RT curvature in Caulobacter.";
RL Mol. Cell 39:975-987(2010).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=NA1000 / CB15N;
RX PubMed=27028265; DOI=10.1111/mmi.13388;
RA Meier E.L., Razavi S., Inoue T., Goley E.D.;
RT "A novel membrane anchor for FtsZ is linked to cell wall hydrolysis in
RT Caulobacter crescentus.";
RL Mol. Microbiol. 101:265-280(2016).
RN [4] {ECO:0007744|PDB:5NR1}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, SUBUNIT, AND INTERACTION
RP WITH FTSZ.
RC STRAIN=NA1000 / CB15N;
RX PubMed=29119622; DOI=10.1111/mmi.13876;
RA Lariviere P.J., Szwedziak P., Mahone C.R., Lowe J., Goley E.D.;
RT "FzlA, an essential regulator of FtsZ filament curvature, controls
RT constriction rate during Caulobacter division.";
RL Mol. Microbiol. 107:180-197(2018).
CC -!- FUNCTION: Essential cell division protein that must bind to FtsZ for
CC division to occur (PubMed:20864042, PubMed:29119622). Critical
CC coordinator of envelope constriction through its interaction with FtsZ
CC (PubMed:29119622). Promotes the formation of highly curved FtsZ
CC filaments, reduces the GTPase activity of FtsZ and stabilizes FtsZ
CC polymers (PubMed:20864042). May regulate FtsZ function by modulating
CC its superstructure (PubMed:20864042). Does not bind to glutathione
CC (PubMed:20864042). {ECO:0000269|PubMed:20864042,
CC ECO:0000269|PubMed:29119622}.
CC -!- SUBUNIT: Homodimer (PubMed:29119622). Interacts with FtsZ filaments
CC (PubMed:20864042, PubMed:29119622). Probably interacts with the GTPase
CC domain of FtsZ (PubMed:29119622). {ECO:0000269|PubMed:20864042,
CC ECO:0000269|PubMed:29119622}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27028265}.
CC Note=Colocalizes with FtsZ at the division site.
CC {ECO:0000269|PubMed:20864042}.
CC -!- INDUCTION: Cell cycle regulated at the transcript and protein levels.
CC mRNA levels peak in predivisional cells. {ECO:0000269|PubMed:20864042}.
CC -!- DISRUPTION PHENOTYPE: Deletion is lethal. Depletion results in cells
CC that are elongated and grow into smooth filaments.
CC {ECO:0000269|PubMed:20864042}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; CP001340; ACL97219.2; -; Genomic_DNA.
DR RefSeq; WP_010921466.1; NC_011916.1.
DR RefSeq; YP_002519127.2; NC_011916.1.
DR PDB; 5NR1; X-ray; 2.00 A; A=1-228.
DR PDBsum; 5NR1; -.
DR AlphaFoldDB; A0A0H3CDY2; -.
DR SMR; A0A0H3CDY2; -.
DR EnsemblBacteria; ACL97219; ACL97219; CCNA_03754.
DR GeneID; 7331950; -.
DR KEGG; ccs:CCNA_03754; -.
DR PATRIC; fig|565050.3.peg.3659; -.
DR HOGENOM; CLU_011226_5_3_5; -.
DR OrthoDB; 1819702at2; -.
DR PhylomeDB; A0A0H3CDY2; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Reference proteome.
FT CHAIN 1..228
FT /note="FtsZ-localized protein A"
FT /id="PRO_0000444996"
FT DOMAIN 3..85
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 90..223
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:5NR1"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:5NR1"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5NR1"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 133..154
FT /evidence="ECO:0007829|PDB:5NR1"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5NR1"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:5NR1"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:5NR1"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:5NR1"
SQ SEQUENCE 228 AA; 26574 MW; 95B817C5958AAD64 CRC64;
MSVERTLHHF PLDPASRQVR LALGEKRLPF VEMQVRYWEM PPEFTSLNPS GMPPVLVETK
HQRNLVICET RAILEHIEET ETEPPLLGRD PAERAEARRL LQWFDRKFDN EVNGFLLHEK
MEKRLLRMGA PDLAALRQGR EALRMHLGYI ESLLQTRDWL AGRRMSLADF AAAAHLSVID
YFGDVPWKDF QAAKTWYMKL KSRPCFRPIL ADRWPGLAPA AHYDDLDF
