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P37_MESHY
ID   P37_MESHY               Reviewed;         403 AA.
AC   P15363;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=High affinity transport system protein p37;
DE   Flags: Precursor;
GN   Name=p37;
OS   Mesomycoplasma hyorhinis (Mycoplasma hyorhinis).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX   NCBI_TaxID=2100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-50.
RX   PubMed=3208756; DOI=10.1002/j.1460-2075.1988.tb03283.x;
RA   Dudler R., Schmidhauser C., Parish R.W., Wettenhall R.E.H., Schmidt T.;
RT   "A mycoplasma high-affinity transport system and the in vitro invasiveness
RT   of mouse sarcoma cells.";
RL   EMBO J. 7:3963-3970(1988).
CC   -!- FUNCTION: P37 is part of a high-affinity transport system.
CC   -!- INTERACTION:
CC       P15363; P07355: ANXA2; Xeno; NbExp=24; IntAct=EBI-12740262, EBI-352622;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
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DR   EMBL; X14140; CAA32357.1; -; Genomic_DNA.
DR   EMBL; M37339; AAA25427.1; -; Genomic_DNA.
DR   PIR; S01828; S01828.
DR   PDB; 3E78; X-ray; 1.90 A; A=1-403.
DR   PDB; 3E79; X-ray; 1.90 A; A=1-403.
DR   PDB; 3EKI; X-ray; 1.60 A; A=1-403.
DR   PDBsum; 3E78; -.
DR   PDBsum; 3E79; -.
DR   PDBsum; 3EKI; -.
DR   AlphaFoldDB; P15363; -.
DR   SMR; P15363; -.
DR   IntAct; P15363; 2.
DR   EvolutionaryTrace; P15363; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IDA:AgBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:AgBase.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IDA:AgBase.
DR   Gene3D; 3.40.190.180; -; 1.
DR   Gene3D; 3.40.190.190; -; 1.
DR   InterPro; IPR010592; CypI.
DR   InterPro; IPR043099; CypI_dom_I.
DR   InterPro; IPR043100; CypI_dom_II.
DR   Pfam; PF06646; Mycoplasma_p37; 1.
DR   PIRSF; PIRSF004523; Mycoplasma_p37; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Direct protein sequencing; Lipoprotein;
KW   Membrane; Palmitate; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:3208756"
FT   CHAIN           24..403
FT                   /note="High affinity transport system protein p37"
FT                   /id="PRO_0000018095"
FT   LIPID           24
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           24
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   STRAND          44..51
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:3E79"
FT   HELIX           64..85
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   TURN            88..92
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          97..104
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           106..114
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          122..125
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          140..152
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           170..182
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   TURN            183..186
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   TURN            192..196
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          217..223
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           225..236
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           240..245
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   TURN            256..259
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           260..269
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   TURN            270..272
FT                   /evidence="ECO:0007829|PDB:3E78"
FT   HELIX           277..283
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           285..287
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           293..298
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          304..308
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           311..314
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          331..337
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          345..349
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           354..369
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           376..379
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   STRAND          383..386
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           390..393
FT                   /evidence="ECO:0007829|PDB:3EKI"
FT   HELIX           395..402
FT                   /evidence="ECO:0007829|PDB:3EKI"
SQ   SEQUENCE   403 AA;  46118 MW;  F924180309DBFFDF CRC64;
     MLKKLKNFIL FSSIFSPIAF AISCSNTGVV KQEDVSVSQG QWDKSITFGV SEAWLNKKKG
     GEKVNKEVIN TFLENFKKEF NKLKNANDKT KNFDDVDFKV TPIQDFTVLL NNLSTDNPEL
     DFGINASGKL VEFLKNNPGI ITPALETTTN SFVFDKEKDK FYVDGTDSDP LVKIAKEINK
     IFVETPYASW TDENHKWNGN VYQSVYDPTV QANFYRGMIW IKGNDETLAK IKKAWNDKDW
     NTFRNFGILH GKDNSFSKFK LEETILKNHF QNKFTTLNED RSAHPNAYKQ KSADTLGTLD
     DFHIAFSEEG SFAWTHNKSA TKPFETKANE KMEALIVTNP IPYDVGVFRK SVNQLEQNLI
     VQTFINLAKN KQDTYGPLLG YNGYKKIDNF QKEIVEVYEK AIK
 
 
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