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TAMB_HAEIN
ID   TAMB_HAEIN              Reviewed;        1298 AA.
AC   Q57523;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Translocation and assembly module subunit TamB;
DE   AltName: Full=Autotransporter assembly factor TamB;
GN   Name=tamB; OrderedLocusNames=HI_0696;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
CC   -!- FUNCTION: Part of the translocation and assembly module (TAM)
CC       autotransporter assembly complex, which functions in translocation of
CC       autotransporters across the outer membrane. Substrate binding to TamA
CC       moves its POTRA domains about 30 Angstroms into the periplasm, which
CC       would deform either the outer membrane or TamB and may provide force to
CC       reset TAM (By similarity). {ECO:0000250|UniProtKB:P39321}.
CC   -!- SUBUNIT: Interacts with TamA. {ECO:0000250|UniProtKB:P39321}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P39321}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P39321}.
CC   -!- DOMAIN: The periplasmic domain is elongated (up to 160 Angstroms long)
CC       and forms contacts to the N-terminal POTRA domains of TamA.
CC       {ECO:0000250|UniProtKB:P39321}.
CC   -!- SIMILARITY: Belongs to the TamB family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22356.1; -; Genomic_DNA.
DR   PIR; A64157; A64157.
DR   RefSeq; NP_438856.1; NC_000907.1.
DR   RefSeq; WP_005694581.1; NC_000907.1.
DR   AlphaFoldDB; Q57523; -.
DR   SMR; Q57523; -.
DR   STRING; 71421.HI_0696; -.
DR   EnsemblBacteria; AAC22356; AAC22356; HI_0696.
DR   KEGG; hin:HI_0696; -.
DR   PATRIC; fig|71421.8.peg.728; -.
DR   eggNOG; COG2911; Bacteria.
DR   HOGENOM; CLU_002338_0_1_6; -.
DR   OMA; NTAKQWP; -.
DR   PhylomeDB; Q57523; -.
DR   BioCyc; HINF71421:G1GJ1-731-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0097347; C:TAM protein secretion complex; IBA:GO_Central.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   InterPro; IPR007452; TamB.
DR   Pfam; PF04357; TamB; 1.
PE   1: Evidence at protein level;
KW   Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1298
FT                   /note="Translocation and assembly module subunit TamB"
FT                   /id="PRO_0000169831"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        28..48
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        49..1298
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1298 AA;  141223 MW;  2D905D8E6D9329E9 CRC64;
     MTEQIQPSET SPKSPEKPNK KHWVRKAVCI GSAVILVPVL GVAGALSFDA GQKSLIQLVD
     KMLDSFSVEQ VEGGLQNGLV LKNVRYQTAG IETHIAQARL QLDFGCLFSR EVCLRDFTLN
     KPTIAINTAL LPPSAPDNSK SGSMKRISLP ISINAENLVM QDLSVNIDQT SITLGNFKSA
     VSLNNEKGLT IAPTEINDIS VIAKKLSEVK SEPKAEQPNK PVDWAAIEQS LTPAFLGNVS
     EIILPFDLHI PEISGKNWQY QAVNEKGETL QSVEMSSLIA QADTVDNQLQ LQKLAVESSL
     GNLSSQGKLQ LDGDMPLDLT LKSHLEPLKS DGKEILPASD VDLTLSGSLK KSTALSLKTK
     GVLDAELNGN VQLAQDKMPL NLTLNVAKGQ YTFVNTMTPL KINDVTLKLT GDLLNYHAEL
     KGDVAGMNYI PASQVELNAD GKLYEVTVNK LGIDSLDGKS EFVGNANWKN GANWDIQADL
     EKMNIAFFVP VMPATLSGKL HSRGFAGSQG WQVEVPVADL NGMLSAKPIS LKGSATLNQN
     VLLTVPDLQI KYGENYLKAS GVLDDHSDFA LDINAPNLRG LWSDLKGRVK GRVAISGQIT
     TPNLDLDLTS SNLHLQGFQL AKASIKGHIN NASLSSGKLN IKAEQLHYGG NIKLHLLDLD
     LSGDEQNHKL ILKSQGEPVA ANLQINGHFD RTLEQWKGTI SQVKFETPIG DVKSNQAIAV
     SYDNKQTQAN IASHCWQNTD VELCFPQAFN AGKQGNIPFQ FKRVNLDLVN KLIEQNSLKG
     NLQVQGNVAW FTDKPFQFTA NVDGNHLAFS QKLDYRTFKL YIPKLTLNAD IQNNNLVLKT
     DINVHNQGRI VGDIHLNDLA KNRQLGGTLA IERLNLSIAN QLLTSGESVN GEVVSKLSFG
     GNLEKPLLNG DFNIRNIRTK LKSMPVNITD GDIALRFNDN RSTLQGKIKT VDSHLNLTGR
     ANWANIEHWT TELNAQANNF NVDIPSMAKL RFSPNITIKA NPKELNLSGT VDIPWARIKI
     DSLPDTAEPV SEDEVILNGP HKSKEELIKR EFAAKTKSGM EIRSDLRINI GKDVSLDAYG
     LKTNLDGLLS VKQDKGNLGL FGQINLTKGR YASFGQDLLI RKGLISFSGQ ATQPTLNIEA
     IRNPETMEDS KITAGVRVIG IADSPEVTIF SEPSKPQDQA LSYLLTGRSL ESSGEVGSTG
     SVGAALIGLG ISKSGKLVGS IGEVFGIQDL NLGTSGVGDK SKVTVSGNIT NRLQIKYGVG
     LFDGLAEVTL RYRLMPQLYF QSVSSTNQVF DLLYKFEF
 
 
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