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MCJD_ECOLX
ID   MCJD_ECOLX              Reviewed;         580 AA.
AC   Q9X2W0;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Microcin-J25 export ATP-binding/permease protein McjD;
DE   AltName: Full=Microcin-J25 immunity protein;
DE   AltName: Full=Microcin-J25 secretion ATP-binding protein McjD;
GN   Name=mcjD;
OS   Escherichia coli.
OG   Plasmid pTUC100.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AY25;
RX   PubMed=10198038; DOI=10.1128/jb.181.8.2659-2662.1999;
RA   Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F.,
RA   Salomon R.A.;
RT   "Sequence analysis of the four plasmid genes required to produce the
RT   circular peptide antibiotic microcin J25.";
RL   J. Bacteriol. 181:2659-2662(1999).
RN   [2]
RP   FUNCTION.
RC   STRAIN=AY25;
RX   PubMed=8655570; DOI=10.1128/jb.178.12.3661-3663.1996;
RA   Solbiati J.O., Ciaccio M., Farias R.N., Salomon R.A.;
RT   "Genetic analysis of plasmid determinants for microcin J25 production and
RT   immunity.";
RL   J. Bacteriol. 178:3661-3663(1996).
CC   -!- FUNCTION: Is able to protect a cell, which harbors the plasmid pTUC100
CC       encoding microcin J25, against microcin J25. Is required for microcin
CC       J25 export out of the producing cells. {ECO:0000269|PubMed:10198038,
CC       ECO:0000269|PubMed:8655570}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AF061787; AAD28497.1; -; Genomic_DNA.
DR   PDB; 4PL0; X-ray; 2.70 A; A/B=1-580.
DR   PDB; 5EG1; X-ray; 3.42 A; A/B=1-580.
DR   PDB; 5OFP; X-ray; 4.71 A; A=1-580.
DR   PDB; 5OFR; X-ray; 3.40 A; A/B=1-580.
DR   PDBsum; 4PL0; -.
DR   PDBsum; 5EG1; -.
DR   PDBsum; 5OFP; -.
DR   PDBsum; 5OFR; -.
DR   AlphaFoldDB; Q9X2W0; -.
DR   SMR; Q9X2W0; -.
DR   TCDB; 3.A.1.118.1; the atp-binding cassette (abc) superfamily.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030153; P:bacteriocin immunity; IEA:UniProtKB-KW.
DR   GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Bacteriocin immunity; Bacteriocin transport;
KW   Cell inner membrane; Cell membrane; Membrane; Nucleotide-binding; Plasmid;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..580
FT                   /note="Microcin-J25 export ATP-binding/permease protein
FT                   McjD"
FT                   /id="PRO_0000092491"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          25..312
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          345..578
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         378..385
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   HELIX           5..8
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           10..15
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           19..53
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:5OFR"
FT   HELIX           59..110
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           122..145
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           148..163
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           167..214
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           216..221
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           225..277
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           283..322
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   TURN            323..325
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          345..368
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          373..377
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           384..391
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          399..404
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           409..411
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           414..420
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          421..424
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          432..434
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           435..440
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           448..457
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          461..463
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           476..478
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           483..496
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          500..506
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   TURN            507..510
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           513..526
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          527..529
FT                   /evidence="ECO:0007829|PDB:5OFR"
FT   STRAND          531..535
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          537..539
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   TURN            540..544
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          545..552
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   STRAND          555..558
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           565..568
FT                   /evidence="ECO:0007829|PDB:4PL0"
FT   HELIX           570..576
FT                   /evidence="ECO:0007829|PDB:4PL0"
SQ   SEQUENCE   580 AA;  65425 MW;  B0F6D0E929F203C6 CRC64;
     MERKQKNSLF NYIYSLMDVR GKFLFFSMLF ITSLSSIIIS ISPLILAKIT DLLSGSLSNF
     SYEYLVLLAC LYMFCVISNK ASVFLFMILQ SSLRINMQKK MSLKYLRELY NENITNLSKN
     NAGYTTQSLN QASNDIYILV RNVSQNILSP VIQLISTIVV VLSTKDWFSA GVFFLYILVF
     VIFNTRLTGS LASLRKHSMD ITLNSYSLLS DTVDNMIAAK KNNALRLISE RYEDALTQEN
     NAQKKYWLLS SKVLLLNSLL AVILFGSVFI YNILGVLNGV VSIGHFIMIT SYIILLSTPV
     ENIGALLSEI RQSMSSLAGF IQRHAENKAT SPSIPFLNME RKLNLSIREL SFSYSDDKKI
     LNSVSLDLFT GKMYSLTGPS GSGKSTLVKI ISGYYKNYFG DIYLNDISLR NISDEDLNDA
     IYYLTQDDYI FMDTLRFNLR LANYDASENE IFKVLKLANL SVVNNEPVSL DTHLINRGNN
     YSGGQKQRIS LARLFLRKPA IIIIDEATSA LDYINESEIL SSIRTHFPDA LIINISHRIN
     LLECSDCVYV LNEGNIVASG HFRDLMVSNE YISGLASVTE
 
 
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