ID   B4EXS4_PROMH            Unreviewed;       339 AA.
AC   B4EXS4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   18-JUN-2025, entry version 101.
DE   RecName: Full=Regulator of RpoS {ECO:0000256|HAMAP-Rule:MF_00958};
GN   Name=rssB {ECO:0000256|HAMAP-Rule:MF_00958};
GN   OrderedLocusNames=PMI1491 {ECO:0000313|EMBL:CAR43129.1};
OS   Proteus mirabilis (strain HI4320).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Morganellaceae; Proteus.
OX   NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR43129.1, ECO:0000313|Proteomes:UP000008319};
RN   [1] {ECO:0000313|EMBL:CAR43129.1, ECO:0000313|Proteomes:UP000008319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI4320 {ECO:0000313|EMBL:CAR43129.1,
RC   ECO:0000313|Proteomes:UP000008319};
RX   PubMed=18375554; DOI=10.1128/JB.01981-07;
RA   Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA   Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA   Parkhill J., Mobley H.L.;
RT   "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT   both adherence and motility.";
RL   J. Bacteriol. 190:4027-4037(2008).
CC   -!- FUNCTION: Regulates the turnover of the sigma S factor (RpoS) by
CC       promoting its proteolysis in exponentially growing cells. Acts by
CC       binding and delivering RpoS to the ClpXP protease. RssB is not co-
CC       degraded with RpoS, but is released from the complex and can initiate a
CC       new cycle of RpoS recognition and degradation. {ECO:0000256|HAMAP-
CC       Rule:MF_00958}.
CC   -!- SUBUNIT: Binds to RpoS. {ECO:0000256|HAMAP-Rule:MF_00958}.
CC   -!- PTM: Phosphorylated. Phosphorylation stimulates the interaction with
CC       RpoS and, therefore, the proteolysis of RpoS. {ECO:0000256|HAMAP-
CC       Rule:MF_00958}.
CC   -!- SIMILARITY: Belongs to the RssB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00958}.
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; AM942759; CAR43129.1; -; Genomic_DNA.
DR   RefSeq; WP_012368013.1; NC_010554.1.
DR   AlphaFoldDB; B4EXS4; -.
DR   EnsemblBacteria; CAR43129; CAR43129; PMI1491.
DR   GeneID; 6801877; -.
DR   KEGG; pmr:PMI1491; -.
DR   eggNOG; COG2197; Bacteria.
DR   HOGENOM; CLU_055989_1_0_6; -.
DR   Proteomes; UP000008319; Chromosome.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   GO; GO:0045862; P:positive regulation of proteolysis; IEA:UniProtKB-UniRule.
DR   GO; GO:0010468; P:regulation of gene expression; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   HAMAP; MF_00958; RssB; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR028616; RssB.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR052048; ST_Response_Regulator.
DR   NCBIfam; NF007969; PRK10693.1; 1.
DR   PANTHER; PTHR43228; TWO-COMPONENT RESPONSE REGULATOR; 1.
DR   PANTHER; PTHR43228:SF1; TWO-COMPONENT RESPONSE REGULATOR ARR22; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00958, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008319};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00958}.
FT   DOMAIN          9..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         59
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00958,
FT                   ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   339 AA;  38951 MW;  3665BD57BD8CE9BD CRC64;
     MNKALVGKKI LIIDDEVVFR TMLTEYFSHE KACVYATDNG SQALLLLEEG LRPDLILCDI
     RMPVMNGPTF LCHLEQRHWS FPVIAISCTD NMAEIDDMLR FGAQDVFLKP VTNLAKLKQK
     VIEVLCPGFF ESELIARGQL GPLWNNLREQ PHYIQSFVKQ MQPQVKQIVA GYNVNYRQLN
     DASQMGLLFD IATLSKDQII FYCVDVSNDE ENGLLVALLL RVVFNRFLKA TEKRRFLPSM
     YNILNKINKM LEDMGVRGSF PLILGYYHTK EKNILLASAG LRAEIKTENK KYVLNSGIPL
     GTLHSLYINQ IKCVGIDWQC KIWNQHHKIN LMFSPIHKR
//