ID V7IG20_SALET Unreviewed; 334 AA.
AC V7IG20;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Cytoskeleton protein RodZ {ECO:0000256|HAMAP-Rule:MF_02017};
GN Name=rodZ {ECO:0000256|HAMAP-Rule:MF_02017};
GN ORFNames=A628_04889 {ECO:0000313|EMBL:ETA85135.1};
OS Salmonella enterica subsp. enterica serovar Cubana str. 76814.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192560 {ECO:0000313|EMBL:ETA85135.1, ECO:0000313|Proteomes:UP000018534};
RN [1] {ECO:0000313|EMBL:ETA85135.1, ECO:0000313|Proteomes:UP000018534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=76814 {ECO:0000313|EMBL:ETA85135.1};
RX PubMed=24459266;
RA Benahmed F.H., Gopinath G.R., Wang H., Jean-Gilles Beaubrun J., Grim C.,
RA Cheng C.M., McClelland M., Ayers S., Abbott J., Desai P., Frye J.G.,
RA Weinstock G., Hammack T.S., Hanes D.E., Rasmussen M.A., Davidson M.K.;
RT "Whole-Genome Sequencing of Salmonella enterica subsp. enterica Serovar
RT Cubana Strains Isolated from Agricultural Sources.";
RL Genome Announc. 2:e01184-13(2014).
CC -!- FUNCTION: Cytoskeletal protein that is involved in cell-shape control
CC through regulation of the length of the long axis. {ECO:0000256|HAMAP-
CC Rule:MF_02017}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02017}; Single-pass type II membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_02017}. Note=Forms helical filaments along
CC the long axis of the cell. {ECO:0000256|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:0000256|HAMAP-Rule:MF_02017}.
CC -!- SIMILARITY: Belongs to the RodZ family. {ECO:0000256|HAMAP-
CC Rule:MF_02017}.
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:ETA85135.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZGR01000172; ETA85135.1; -; Genomic_DNA.
DR RefSeq; WP_001090898.1; NZ_KI635663.1.
DR AlphaFoldDB; V7IG20; -.
DR SMR; V7IG20; -.
DR PATRIC; fig|1192560.4.peg.4513; -.
DR HOGENOM; CLU_047530_3_1_6; -.
DR Proteomes; UP000018534; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_02017};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_02017};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_02017}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02017};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968, ECO:0000256|HAMAP-
KW Rule:MF_02017};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02017};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02017}.
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02017"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 133..334
FT /note="Periplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02017"
FT DOMAIN 19..54
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT DNA_BIND 30..49
FT /note="H-T-H motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02017"
FT REGION 154..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 35802 MW; B2BA2266A64D9A3C CRC64;
MNTEATHDQN EAQTTGVRLR NAREQLGLSQ QAVAERLCLK VSTVRDIEED KAPSDLASTF
LRGYIRSYAR LVHVPEEELL PGLEKQAPLR AAKVAPMQSF SLGKRRKKRD GWLMSFTWLV
LFVVVGLTGA WWWQNHKAQQ EEITTMADQS TAELNADKDS GQSVPLDTRD ATSQDTTPAQ
TAPAPATPVD STAATQTPAP TAAATQNTVV APSQANVDTA ATSAAPAATE TPSALPTSQA
GVAAPAADPN ALVMNFTADC WLEVTDATGK KLFSGMQRKD GNLNLTGQAP YKLKIGAPAA
VQIQYQGKPV DLSRFIRTNQ VARLTLNAEP TPAQ
//
