ID RODZ_ECOLU Reviewed; 337 AA.
AC B7N6A4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Cytoskeleton protein RodZ {ECO:0000255|HAMAP-Rule:MF_02017};
GN Name=rodZ {ECO:0000255|HAMAP-Rule:MF_02017}; OrderedLocusNames=ECUMN_2836;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Cytoskeletal protein that is involved in cell-shape control
CC through regulation of the length of the long axis. {ECO:0000255|HAMAP-
CC Rule:MF_02017}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02017}; Single-pass type II membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02017}. Note=Forms helical filaments along
CC the long axis of the cell. {ECO:0000255|HAMAP-Rule:MF_02017}.
CC -!- DOMAIN: The helix-turn-helix (HTH) motif in the cytoplasmic domain of
CC the N-terminus is involved in the formation of spirals to maintain the
CC rigid rod shape. As this protein is anchored in the cytoplasmic
CC membrane, the HTH motif may contribute to protein-protein interactions
CC to form the RodZ helix, which is localized beneath the cytoplasmic
CC membrane. The C-terminal domain may be critical for determination of
CC the rod shape by probably interacting with enzymes required for
CC synthesis of the peptidoglycan layer, including PBPs in the periplasm.
CC {ECO:0000255|HAMAP-Rule:MF_02017}.
CC -!- SIMILARITY: Belongs to the RodZ family. {ECO:0000255|HAMAP-
CC Rule:MF_02017}.
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DR EMBL; CU928163; CAR14013.1; -; Genomic_DNA.
DR RefSeq; WP_001090848.1; NC_011751.1.
DR RefSeq; YP_002413538.1; NC_011751.1.
DR AlphaFoldDB; B7N6A4; -.
DR SMR; B7N6A4; -.
DR STRING; 585056.ECUMN_2836; -.
DR KEGG; eum:ECUMN_2836; -.
DR PATRIC; fig|585056.7.peg.3021; -.
DR HOGENOM; CLU_047530_3_1_6; -.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1.
DR HAMAP; MF_02017; RodZ; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR023690; RodZ.
DR InterPro; IPR025194; RodZ-like_C.
DR PANTHER; PTHR34475; -; 1.
DR PANTHER; PTHR34475:SF1; CYTOSKELETON PROTEIN RODZ; 1.
DR Pfam; PF13413; HTH_25; 1.
DR Pfam; PF13464; RodZ_C; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell shape; DNA-binding; Membrane;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..337
FT /note="Cytoskeleton protein RodZ"
FT /id="PRO_1000189542"
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT TRANSMEM 112..132
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT TOPO_DOM 133..337
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT DOMAIN 19..71
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT DNA_BIND 30..49
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02017"
FT REGION 145..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 337 AA; 36187 MW; 8CEA1A7E5E8CD87A CRC64;
MNTEATHDQN EALTTGARLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPADLASTF
LRGYIRSYAR LVHIPEEELL PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMTFTWLV
LFVVIGLSGA WWWQDHKAQQ EEITTMADQS SAELSSNSEQ GQSVPLNTST TTDPATTSTP
PASVDTTATN TQTPAVTAPA PAVDPQQNAV VSPSQANVDT AATPAPTATI TPDGAAPLPT
DQAGVTTPAA DPNALVMNFT ADCWLEVTDA TGKKLFSGMQ RKDGNLNLTG QAPYKLKIGA
PAAVQIQYQG KPVDLSRFIR TNQVARLTLN AEQSPAQ
//
