CREN1_PYRCJ
ID CREN1_PYRCJ Reviewed; 432 AA.
AC A3MWN5;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Crenactin {ECO:0000303|PubMed:21414041};
DE AltName: Full=Archaeal actin homolog {ECO:0000303|PubMed:21414041};
GN Name=cren-1 {ECO:0000303|PubMed:21414041};
GN OrderedLocusNames=Pcal_1635 {ECO:0000312|EMBL:ABO09052.1};
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=21414041; DOI=10.1111/j.1365-2958.2011.07635.x;
RA Ettema T.J., Lindaas A.C., Bernander R.;
RT "An actin-based cytoskeleton in archaea.";
RL Mol. Microbiol. 80:1052-1061(2011).
RN [3]
RP SUBUNIT.
RX PubMed=26124094; DOI=10.1073/pnas.1509069112;
RA Braun T., Orlova A., Valegaard K., Lindaas A.C., Schroeder G.F.,
RA Egelman E.H.;
RT "Archaeal actin from a hyperthermophile forms a single-stranded filament.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:9340-9345(2015).
RN [4] {ECO:0007744|PDB:4BQL}
RP X-RAY CRYSTALLOGRAPHY (3.34 ANGSTROMS) IN COMPLEX WITH ADP, AND SUBUNIT.
RX PubMed=24531483; DOI=10.1107/s1399004714000935;
RA Lindas A.C., Chruszcz M., Bernander R., Valegard K.;
RT "Structure of crenactin, an archaeal actin homologue active at 90C.";
RL Acta Crystallogr. D 70:492-500(2014).
RN [5] {ECO:0007744|PDB:4CJ7}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH ADP, AND SUBUNIT.
RX PubMed=24486010; DOI=10.1016/j.febslet.2014.01.029;
RA Izore T., Duman R., Kureisaite-Ciziene D., Lowe J.;
RT "Crenactin from Pyrobaculum calidifontis is closely related to actin in
RT structure and forms steep helical filaments.";
RL FEBS Lett. 588:776-782(2014).
RN [6] {ECO:0007744|PDB:5LY3}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH ADP AND ARCADIN-2
RP C-TERMINUS, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH ARCADIN-1
RP AND ARCADIN-2.
RX PubMed=27852434; DOI=10.7554/elife.21600;
RA Izore T., Kureisaite-Ciziene D., McLaughlin S.H., Lowe J.;
RT "Crenactin forms actin-like double helical filaments regulated by arcadin-
RT 2.";
RL Elife 5:E21600-E21600(2016).
CC -!- FUNCTION: Forms the backbone of an actin-like archaeal cytoskeleton,
CC which is involved in cell shape determination. Has ATPase activity.
CC Shows highest activity towards ATP or GTP as nucleotide, and only
CC residual activity on UTP, CTP and dNTPs. {ECO:0000269|PubMed:21414041}.
CC -!- ACTIVITY REGULATION: Crenactin polymerization is inhibited by
CC interaction with arcadin-2 (PubMed:27852434). Also significantly
CC inhibited by elevated antibiotic A22 concentrations (PubMed:21414041).
CC {ECO:0000269|PubMed:21414041, ECO:0000269|PubMed:27852434}.
CC -!- SUBUNIT: Monomer. The crenactin monomers polymerize into right-handed
CC helical filaments, with 8 subunits per complete turn of the helix
CC (PubMed:24531483, PubMed:24486010). Forms single-stranded filaments
CC under high salt concentrations and double-stranded filaments under low
CC salt concentrations (PubMed:26124094, PubMed:27852434). Interacts with
CC arcadin-1 and arcadin-2 (PubMed:27852434).
CC {ECO:0000269|PubMed:24486010, ECO:0000269|PubMed:24531483,
CC ECO:0000269|PubMed:26124094, ECO:0000269|PubMed:27852434}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Note=Forms
CC cell-spanning helical structures. {ECO:0000269|PubMed:21414041}.
CC -!- MISCELLANEOUS: Belongs to a conserved five-gene operon within
CC Thermoproteales denoted Arcade (actin-related cytoskeleton in Archaea
CC involved in shape determination). {ECO:0000305|PubMed:21414041}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; CP000561; ABO09052.1; -; Genomic_DNA.
DR PDB; 4BQL; X-ray; 3.34 A; A/B/C/D=1-432.
DR PDB; 4CJ7; X-ray; 3.20 A; A/B=1-432.
DR PDB; 5LY3; X-ray; 1.60 A; A=1-432.
DR PDB; 5MW1; EM; 3.80 A; A/B/C/D/E/F=1-432.
DR PDBsum; 4BQL; -.
DR PDBsum; 4CJ7; -.
DR PDBsum; 5LY3; -.
DR PDBsum; 5MW1; -.
DR AlphaFoldDB; A3MWN5; -.
DR SMR; A3MWN5; -.
DR STRING; 410359.Pcal_1635; -.
DR EnsemblBacteria; ABO09052; ABO09052; Pcal_1635.
DR KEGG; pcl:Pcal_1635; -.
DR eggNOG; arCOG05583; Archaea.
DR HOGENOM; CLU_627936_0_0_2; -.
DR OMA; WTRFLIG; -.
DR Proteomes; UP000001431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
FT CHAIN 1..432
FT /note="Crenactin"
FT /id="PRO_0000439071"
FT BINDING 20..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24486010,
FT ECO:0000305|PubMed:24531483, ECO:0000305|PubMed:27852434"
FT BINDING 182..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24486010,
FT ECO:0000305|PubMed:24531483, ECO:0000305|PubMed:27852434"
FT BINDING 235..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24486010,
FT ECO:0000305|PubMed:24531483, ECO:0000305|PubMed:27852434"
FT BINDING 354..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:24486010,
FT ECO:0000305|PubMed:24531483, ECO:0000305|PubMed:27852434"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:27852434"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4BQL"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:4BQL"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4CJ7"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:4BQL"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 187..196
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 248..257
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:4BQL"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 371..382
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:5LY3"
FT HELIX 401..412
FT /evidence="ECO:0007829|PDB:5LY3"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:5LY3"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:4CJ7"
SQ SEQUENCE 432 AA; 48369 MW; 9F505AD5041DFE86 CRC64;
MGVISDAYRL KYTFGVDFGT SYVKYGPITL NEPKMVQTRG LFLRDLPESV KMRIPPDVLA
RGLVVGDEEV RKYLSSVRDV QRNLKYPLKD GVARRDDEEA WRVLKELARY TLAQFPVSDP
EFAGWLVAVA LSALAPDYMY KAIFDIYDEL ASEFKIYAVT ILPQPLAVAI AENAVNCVIV
EGGHGNIQVA PISFALIREG LVALNRGGAE ANAITREILK DIGYSDIARE EYAVEVVKRA
VGLVPRRLKE AIRAAKSDPD RFVTKVRLSP VVEVEIPREY AWTRFLIGEI VFDPNHEEIK
SYIEQSRLRI ENAVIGDVTL YGEMDVASAI ITSLRNVSVE IQERVASQII LSGGAFSWRV
PPGMEDVAAD SVTRVKIALE EKSPALASKV EVRLVSEPQY SVWRGAVIYG YALPLSLEWS
DTTREGWRFP RR
