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TONB_PSEAE
ID   TONB_PSEAE              Reviewed;         342 AA.
AC   Q51368;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Protein TonB;
GN   Name=tonB; OrderedLocusNames=PA5531;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=8704984; DOI=10.1099/13500872-142-6-1449;
RA   Poole K., Zhao Q., Neshat S., Heinrichs D.E., Dean C.R.;
RT   "The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein.";
RL   Microbiology 142:1449-1458(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Interacts with outer membrane receptor proteins that carry
CC       out high-affinity binding and energy dependent uptake into the
CC       periplasmic space of specific substrates. It could act to transduce
CC       energy from the cytoplasmic membrane to specific energy-requiring
CC       processes in the outer membrane, resulting in the release into the
CC       periplasm of ligands bound by these outer membrane proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Forms a complex with the accessory proteins ExbB
CC       and ExbD (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TonB family. {ECO:0000305}.
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DR   EMBL; U23764; AAB18654.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG08916.1; -; Genomic_DNA.
DR   PIR; E82955; E82955.
DR   RefSeq; NP_254218.1; NC_002516.2.
DR   RefSeq; WP_010895710.1; NZ_QZGE01000012.1.
DR   PDB; 6FIP; NMR; -; A=247-342.
DR   PDB; 6I97; X-ray; 3.35 A; D/E=251-340.
DR   PDBsum; 6FIP; -.
DR   PDBsum; 6I97; -.
DR   AlphaFoldDB; Q51368; -.
DR   BMRB; Q51368; -.
DR   SMR; Q51368; -.
DR   STRING; 287.DR97_2910; -.
DR   PaxDb; Q51368; -.
DR   PRIDE; Q51368; -.
DR   EnsemblBacteria; AAG08916; AAG08916; PA5531.
DR   GeneID; 878138; -.
DR   KEGG; pae:PA5531; -.
DR   PATRIC; fig|208964.12.peg.5796; -.
DR   PseudoCAP; PA5531; -.
DR   HOGENOM; CLU_811022_0_0_6; -.
DR   InParanoid; Q51368; -.
DR   OMA; SEAQAYN; -.
DR   BioCyc; PAER208964:G1FZ6-5658-MON; -.
DR   PHI-base; PHI:6942; -.
DR   PHI-base; PHI:8066; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0098797; C:plasma membrane protein complex; IBA:GO_Central.
DR   GO; GO:0031992; F:energy transducer activity; IBA:GO_Central.
DR   GO; GO:0015343; F:siderophore transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IMP:PseudoCAP.
DR   GO; GO:0071236; P:cellular response to antibiotic; IMP:PseudoCAP.
DR   GO; GO:0033212; P:iron import into cell; IMP:PseudoCAP.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:PseudoCAP.
DR   GO; GO:0043107; P:type IV pilus-dependent motility; IMP:PseudoCAP.
DR   InterPro; IPR003538; TonB.
DR   InterPro; IPR006260; TonB/TolA_C.
DR   InterPro; IPR037682; TonB_C.
DR   Pfam; PF03544; TonB_C; 1.
DR   PRINTS; PR01374; TONBPROTEIN.
DR   TIGRFAMs; TIGR01352; tonB_Cterm; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Protein transport; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..342
FT                   /note="Protein TonB"
FT                   /id="PRO_0000196207"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..342
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          157..158
FT                   /note="1"
FT   REPEAT          159..160
FT                   /note="2"
FT   REPEAT          161..162
FT                   /note="3"
FT   REPEAT          164..165
FT                   /note="4"
FT   REPEAT          166..167
FT                   /note="5"
FT   REPEAT          168..169
FT                   /note="6; approximate"
FT   REPEAT          170..171
FT                   /note="7"
FT   REPEAT          172..173
FT                   /note="8"
FT   REPEAT          174..175
FT                   /note="9"
FT   REPEAT          176..177
FT                   /note="10"
FT   REPEAT          178..179
FT                   /note="11"
FT   REPEAT          180..181
FT                   /note="12"
FT   REPEAT          190..191
FT                   /note="13"
FT   REPEAT          192..193
FT                   /note="14"
FT   REPEAT          194..195
FT                   /note="15"
FT   REPEAT          196..197
FT                   /note="16"
FT   REPEAT          198..199
FT                   /note="17"
FT   REPEAT          202..203
FT                   /note="18"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          157..203
FT                   /note="18 X 2 approximate repeats of [KE]-P"
FT   COMPBIAS        154..201
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        272
FT                   /note="G -> R (in Ref. 1; AAB18654)"
FT                   /evidence="ECO:0000305"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   HELIX           266..269
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   TURN            270..272
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   STRAND          275..283
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   STRAND          287..299
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   HELIX           304..313
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   STRAND          315..317
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   STRAND          322..326
FT                   /evidence="ECO:0007829|PDB:6I97"
FT   STRAND          329..338
FT                   /evidence="ECO:0007829|PDB:6I97"
SQ   SEQUENCE   342 AA;  36892 MW;  157F036B39E9152D CRC64;
     MSPQPSRSPD RFSLAALAED HPTAPAQGDE SESLPCVNAQ RGEPNLRVVD CSGARRDEEV
     AVEEVLIPYA HGSDPEDVPG EPPKSRWWLS SGAAVAMHVA IIGALVWVMP TPAELNLGHG
     ELPKTMQVNF VQLEKKAEPT PQPPAAAPEP TPPKIEEPKP EPPKPKPVEK PKPKPKPKPK
     PVENAIPKAK PKPEPKPKPE PEPSTEASSQ PSPSSAAPPP APTVGQSTPG AQTAPSGSQG
     PAGLPSGSLN DSDIKPLRMD PPVYPRMAQA RGIEGRVKVL FTITSDGRID DIQVLESVPS
     RMFDREVRQA MAKWRFEPRV SGGKIVARQA TKMFFFKIEK RR
 
 
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