ID   YMOA_YEREN              Reviewed;          67 AA.
AC   P0A3X1; P27720;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Modulating protein YmoA;
DE   AltName: Full=Histone-like protein;
GN   Name=ymoA; Synonyms=hha;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=W227 / Serotype O:9;
RX   PubMed=1956283; DOI=10.1111/j.1365-2958.1991.tb01875.x;
RA   Cornelis G.R., Sluiters C., Delor I., Geib D., Kaniga K.,
RA   Lambert de Rouvroit C., Sory M.-P., Vanooteghem J.-C., Michiels T.;
RT   "ymoA, a Yersinia enterocolitica chromosomal gene modulating the expression
RT   of virulence functions.";
RL   Mol. Microbiol. 5:1023-1034(1991).
RN   [2]
RP   SIMILARITY TO HHA.
RX   PubMed=1484495; DOI=10.1111/j.1365-2958.1992.tb02214.x;
RA   de la Cruz F., Carmona M., Juarez A.;
RT   "The Hha protein from Escherichia coli is highly homologous to the YmoA
RT   protein from Yersinia enterocolitica.";
RL   Mol. Microbiol. 6:3451-3452(1992).
RN   [3]
RP   INTERACTION WITH H-NS.
RC   STRAIN=DSM 9499 / NCTC 11174 / Y754;
RX   PubMed=11790731; DOI=10.1128/jb.184.3.629-635.2002;
RA   Nieto J.M., Madrid C., Miquelay E., Parra J.L., Rodriguez S., Juarez A.;
RT   "Evidence for direct protein-protein interaction between members of the
RT   enterobacterial Hha/YmoA and H-NS families of proteins.";
RL   J. Bacteriol. 184:629-635(2002).
RN   [4]
RP   SUBUNIT, AND MUTAGENESIS OF ASP-43.
RX   PubMed=26085102; DOI=10.1074/jbc.m114.630400;
RA   Cordeiro T.N., Garcia J., Bernado P., Millet O., Pons M.;
RT   "A three-protein charge zipper stabilizes a complex modulating bacterial
RT   gene silencing.";
RL   J. Biol. Chem. 290:21200-21212(2015).
CC   -!- FUNCTION: Modulates the thermoregulation of VirF, and hence the yop
CC       regulon, as well as the expression of the enterotoxin gene yst
CC       (PubMed:1956283). Involved in chromosome structure and DNA topology
CC       probably by means of compaction of DNA in conjunction with H-NS;
CC       probably requires H-NS to bind DNA (By similarity).
CC       {ECO:0000250|UniProtKB:P0ACE3, ECO:0000269|PubMed:1956283}.
CC   -!- SUBUNIT: Interacts with H-NS, in the absence of DNA (PubMed:11790731,
CC       PubMed:26085102). {ECO:0000269|PubMed:11790731,
CC       ECO:0000269|PubMed:26085102}.
CC   -!- SIMILARITY: Belongs to the Hha/YmoA/Cnu family.
CC       {ECO:0000305|PubMed:1484495}.
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DR   EMBL; X58058; CAA41091.1; -; Genomic_DNA.
DR   PIR; S15291; S15291.
DR   RefSeq; WP_002208622.1; NZ_UHIX01000001.1.
DR   AlphaFoldDB; P0A3X1; -.
DR   BMRB; P0A3X1; -.
DR   SMR; P0A3X1; -.
DR   STRING; 1443113.LC20_01418; -.
DR   GeneID; 61907009; -.
DR   GeneID; 67420002; -.
DR   eggNOG; ENOG5032SGA; Bacteria.
DR   OMA; RRCQSID; -.
DR   OrthoDB; 1919885at2; -.
DR   Gene3D; 1.20.1280.40; -; 1.
DR   InterPro; IPR007985; Hemolysn_expr_modulating_HHA.
DR   InterPro; IPR036666; HHA_sf.
DR   Pfam; PF05321; HHA; 1.
DR   SUPFAM; SSF68989; SSF68989; 1.
PE   1: Evidence at protein level;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..67
FT                   /note="Modulating protein YmoA"
FT                   /id="PRO_0000201731"
FT   MUTAGEN         43
FT                   /note="D->N: Alters structural dynamics of free protein,
FT                   loss of H-NS binding (tested with E.coli H-NS fragment 1-
FT                   64)."
FT                   /evidence="ECO:0000269|PubMed:26085102"
SQ   SEQUENCE   67 AA;  8063 MW;  F74388E5E14F294F CRC64;
     MTKTDYLMRL RKCTTIDTLE RVIEKNKYEL SDDELELFYS AADHRLAELT MNKLYDKIPP
     TVWQHVK