ID   RODZ_STRR6              Reviewed;         276 AA.
AC   Q8DMX7;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Cytoskeleton protein RodZ {ECO:0000303|PubMed:28710862};
GN   Name=rodZ {ECO:0000303|PubMed:28710862}; OrderedLocusNames=spr2028;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND TOPOLOGY.
RC   STRAIN=R6 / R704;
RX   PubMed=28710862; DOI=10.1111/mmi.13748;
RA   Stamsaas G.A., Straume D., Ruud Winther A., Kjos M., Frantzen C.A.,
RA   Haavarstein L.S.;
RT   "Identification of EloR (Spr1851) as a regulator of cell elongation in
RT   Streptococcus pneumoniae.";
RL   Mol. Microbiol. 105:954-967(2017).
RN   [3]
RP   FUNCTION, INTERACTION WITH KHPB, AND DISRUPTION PHENOTYPE.
RC   STRAIN=R6 / R704;
RX   PubMed=33558392; DOI=10.1128/jb.00691-20;
RA   Winther A.R., Kjos M., Herigstad M.L., Haavarstein L.S., Straume D.;
RT   "EloR interacts with the lytic transglycosylase MltG at midcell in
RT   Streptococcus pneumoniae R6.";
RL   J. Bacteriol. 0:0-0(2021).
CC   -!- FUNCTION: Cytoskeletal protein that is involved in cell-shape control
CC       through regulation of the length of the long axis (By similarity).
CC       Probably part of the elongasome which synthesizes peripheral
CC       peptidogylcan (Probable). {ECO:0000250|UniProtKB:P27434,
CC       ECO:0000305|PubMed:28710862, ECO:0000305|PubMed:33558392}.
CC   -!- SUBUNIT: Interacts with MltG and MreC in the elongasome
CC       (PubMed:28710862). Interacts with KhpB (also called EloR/Jag)
CC       (PubMed:33558392). {ECO:0000269|PubMed:28710862,
CC       ECO:0000269|PubMed:33558392}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Cells are smaller. Deletion suppresses activating
CC       mutations in khpB (also called eloR/jag) (PubMed:28710862). No change
CC       in subcellular location of KhpB (PubMed:33558392).
CC       {ECO:0000269|PubMed:28710862, ECO:0000269|PubMed:33558392}.
CC   -!- SIMILARITY: Belongs to the RodZ family. {ECO:0000305}.
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DR   EMBL; AE007317; AAL00830.1; -; Genomic_DNA.
DR   PIR; A99525; A99525.
DR   PIR; F95259; F95259.
DR   RefSeq; NP_359619.1; NC_003098.1.
DR   AlphaFoldDB; Q8DMX7; -.
DR   STRING; 171101.spr2028; -.
DR   EnsemblBacteria; AAL00830; AAL00830; spr2028.
DR   KEGG; spr:spr2028; -.
DR   PATRIC; fig|171101.6.peg.2194; -.
DR   eggNOG; COG1426; Bacteria.
DR   HOGENOM; CLU_047530_0_2_9; -.
DR   OMA; LRKYAWA; -.
DR   PHI-base; PHI:3158; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   SUPFAM; SSF47413; SSF47413; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell shape; Membrane; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..276
FT                   /note="Cytoskeleton protein RodZ"
FT                   /id="PRO_0000454550"
FT   TOPO_DOM        1..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:28710862"
FT   TRANSMEM        111..131
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..276
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:28710862"
SQ   SEQUENCE   276 AA;  30551 MW;  19091651DFDFBE29 CRC64;
     MTSMRKKTIG EVLRLARINQ GLSLDELQKK TEIQLDMLEA MEADDFDQLP SPFYTRSFLK
     KYAWAVELDD QIVLDAYDSG SMITYEEVDV DEDELTGRRR SSKKKKKKTS FLPLFYFILF
     ALSILIFVTY YVWNYIQTQP EEPSLSNYSV VQSTSSTSSV PHSSSSSSSS IESAISVSGE
     GNHVEIAYKT SKETVKLQLA VSDVTSWVSV SESELEGGVT LSPKKKSAEA TVATKSPVTI
     TLGVVKGVDL TVDNQTVDLS KLTAQTGQIT VTFTKN