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Database: UniProt
Entry: Q31T92_SHIBS
LinkDB: Q31T92_SHIBS
Original site: Q31T92_SHIBS 
ID   Q31T92_SHIBS            Unreviewed;      1107 AA.
AC   Q31T92;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Periplasmic binding protein {ECO:0000313|EMBL:ABB68716.1};
GN   Name=yjeP {ECO:0000313|EMBL:ABB68716.1};
GN   OrderedLocusNames=SBO_4298 {ECO:0000313|EMBL:ABB68716.1};
OS   Shigella boydii serotype 4 (strain Sb227).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300268 {ECO:0000313|EMBL:ABB68716.1, ECO:0000313|Proteomes:UP000007067};
RN   [1] {ECO:0000313|EMBL:ABB68716.1, ECO:0000313|Proteomes:UP000007067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sb227 {ECO:0000313|EMBL:ABB68716.1,
RC   ECO:0000313|Proteomes:UP000007067};
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC       {ECO:0000256|ARBA:ARBA00008017}.
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DR   EMBL; CP000036; ABB68716.1; -; Genomic_DNA.
DR   RefSeq; WP_001236840.1; NC_007613.1.
DR   AlphaFoldDB; Q31T92; -.
DR   KEGG; sbo:SBO_4298; -.
DR   HOGENOM; CLU_007829_2_0_6; -.
DR   Proteomes; UP000007067; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.10.287.1260; -; 1.
DR   Gene3D; 2.30.30.60; -; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR049142; MS_channel_1st.
DR   InterPro; IPR049278; MS_channel_C.
DR   InterPro; IPR023408; MscS_beta-dom_sf.
DR   InterPro; IPR006685; MscS_channel_2nd.
DR   InterPro; IPR011066; MscS_channel_C_sf.
DR   InterPro; IPR006686; MscS_channel_CS.
DR   InterPro; IPR011014; MscS_channel_TM-2.
DR   InterPro; IPR025692; MscS_IM_dom1.
DR   InterPro; IPR024393; MscS_porin.
DR   PANTHER; PTHR30347:SF1; MINICONDUCTANCE MECHANOSENSITIVE CHANNEL MSCM; 1.
DR   PANTHER; PTHR30347; POTASSIUM CHANNEL RELATED; 1.
DR   Pfam; PF21088; MS_channel_1st; 1.
DR   Pfam; PF00924; MS_channel_2nd; 1.
DR   Pfam; PF21082; MS_channel_3rd; 1.
DR   Pfam; PF12795; MscS_porin; 1.
DR   Pfam; PF12794; MscS_TM; 1.
DR   SUPFAM; SSF82689; Mechanosensitive channel protein MscS (YggB), C-terminal domain; 1.
DR   SUPFAM; SSF82861; Mechanosensitive channel protein MscS (YggB), transmembrane region; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS01246; UPF0003; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1107
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004220273"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        517..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        551..576
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        597..617
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        670..691
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        697..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        785..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        828..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        879..897
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        903..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..255
FT                   /note="Mechanosensitive ion channel MscS porin"
FT                   /evidence="ECO:0000259|Pfam:PF12795"
FT   DOMAIN          478..814
FT                   /note="Mechanosensitive ion channel inner membrane"
FT                   /evidence="ECO:0000259|Pfam:PF12794"
FT   DOMAIN          875..916
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          918..983
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          991..1074
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
FT   COILED          121..158
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          196..238
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1107 AA;  123950 MW;  5F52F78D6B94532B CRC64;
     MRLIITFLMA WCLSWGAYAA TAPDSKQITQ ELEQAKAAKP AQPEVVEALQ SALNALEERK
     GSLERIKQYQ QVIDNYPKLS ATLRAQLNNI RDEPRSVSPG MSTDALNQEI LQVSSQLLDK
     SRQAQQEQER AREIADSLNQ LPQQQTDARR QLNEIERRLG TLTGNTPLNQ AQNFALQSDS
     ARLKALVDEL ELAQLSANNR QELARLRSEL AEKESQQLDA YLQALRNQLN SQRQLEAERA
     LESTELLAEN SADLPKDIVA QFKINRELSA ALNQQAQRMD LVASQQRQAA SQTLQVRQAL
     NTLREQSQWL GSSNLLGEAL RAQVARLPEM PKPQQLDTEM AQLRVQRLRY EDLLNKQPLL
     RQIHQADGQP LTAEQNRILE AQLRTQRELL NSLLQGGDTL LLELTKLKVS NGQLEDALKE
     VNEATHRYLF WTSDVRPMTI AWPLEIAQDL RRLISLDTFS QLGKASVMML TSKETILPLF
     GALILVGCSI YSRRYFTRFL ERSAAKVGKV TQDHFWLTLR TLFWSILVAS PLPVLWMTLG
     YGLREAWPYP LAVAIGDGVT ATVPLLWVVM ICATFARPNG LFIAHFGWPR ERVSRGMRYY
     LMSIGLIVPL IMALMMFDNL DDREFSGSLG RLCFILICGA LAVVTLSLKK AGIPLYLNKE
     GSGDNITNHM LWNMMIGAPL VAILASAVGY LATAQALLAR LETSVAIWFL LLVVYHVIRR
     WMLIQRRRLA FDRAKHRRAE MLAQRARGEE EAHHHSSPEG AIEVDESEVD LDAISAQSLR
     LVRSILMLIA LLSVIVLWSE IHSAFGFLEN ISLWDVTSTV QGVESLEPIT LGAVLIAILV
     FIITTQLVRN LPALLELAIL QHLDLTPGTG YAITTITKYL LMLIGGLVGF SMIGIEWSKL
     QWLVAALGVG LGFGLQEIFA NFISGLIILF EKPIRIGDTV TIRDLTGSVT KINTRATTIS
     DWDRKEIIVP NKAFITEQFI NWSLSDSVTR VVLTIPAPAD ANSEEVTEIL LTAARRCSLV
     IDNPAPEVFL VDLQQGIQIF ELRIYAAEMG HRMPLRHEIH QLILAGFHAH GIDMPFPPFQ
     MRLESLNGKQ TGRTLTSAGK GRQAGSL
//
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