(data stored in ACNUC7421 zone)

HOGENOM: ECOBB_1_PE100

ID   ECOBB_1_PE100                        STANDARD;      PRT;   901 AA.
AC   ECOBB_1_PE100; C6EAV7; C5W347;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Protein translocase subunit SecA; (ECOBB_1.PE100).
GN   Name=secA; OrderedLocusNames=B21_00098, ECBD_3519, ECD_00099;
OS   ESCHERICHIA COLI BL21.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=511693;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOBB_1.PE100.
CC       Escherichia coli (strain B / BL21) chromosome, complete sequence.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C6EAV7_ECOBD
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. Has a central role
CC       in coupling the hydrolysis of ATP to the transfer of proteins into
CC       and across the cell membrane, serving both as a receptor for the
CC       preprotein-SecB complex and as an ATP-driven molecular motor
CC       driving the stepwise translocation of polypeptide chains across
CC       the membrane (By similarity).
CC   -!- COFACTOR: May bind 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDFyajC and YidC(OxaA) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50
CC       (By similarity).
CC   -!- INDUCTION: Repressed under conditions of excess protein secretion
CC       capacity and derepressed when protein secretion becomes limiting.
CC       This is regulated by SecM (By similarity).
CC   -!- SIMILARITY: Belongs to the SecA family.
CC   -!- SIMILARITY: Belongs to the secA family.
CC   -!- GENE_FAMILY: HOG000218168 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6EAV7; C5W347; -.
DR   EMBL; CP001665; ACT30518.1; -; Genomic_DNA.
DR   EMBL; CP001509; ACT42000.1; -; Genomic_DNA.
DR   EMBL; AM946981; CAQ30615.1; -; Genomic_DNA.
DR   ProteinModelPortal; C6EAV7; -.
DR   SMR; C6EAV7; 9-836.
DR   STRING; C6EAV7; -.
DR   PRIDE; C6EAV7; -.
DR   EnsemblBacteria; EBESCT00000159142; EBESCP00000147057; EBESCG00000155259.
DR   EnsemblBacteria; EBESCT00000188796; EBESCP00000176426; EBESCG00000190533.
DR   EnsemblBacteria; EBESCT00000195360; EBESCP00000179709; EBESCG00000193277.
DR   GenomeReviews; AM946981_GR; B21_00098.
DR   GenomeReviews; CP001509_GR; ECD_00099.
DR   GenomeReviews; CP001665_GR; ECBD_3519.
DR   KEGG; ebd:ECBD_3519; -.
DR   GeneTree; EBGT00050000010701; -.
DR   OMA; GGMVLHD; -.
DR   ProtClustDB; PRK12904; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:HAMAP.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:HAMAP.
DR   HAMAP; MF_01382; SecA; 1; -.
DR   InterPro; IPR004027; SEC_C_motif.
DR   InterPro; IPR000185; SecA.
DR   InterPro; IPR020937; SecA_CS.
DR   InterPro; IPR011115; SecA_DEAD.
DR   InterPro; IPR014018; SecA_motor_DEAD.
DR   InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR   InterPro; IPR011116; SecA_Wing/Scaffold.
DR   Gene3D; G3DSA:3.90.1440.10; G3DSA:3.90.1440.10; 1.
DR   Gene3D; G3DSA:1.10.3060.10; SecA_SW; 1.
DR   Pfam; PF02810; SEC-C; 1.
DR   Pfam; PF07517; SecA_DEAD; 1.
DR   Pfam; PF01043; SecA_PP_bind; 1.
DR   Pfam; PF07516; SecA_SW; 1.
DR   PRINTS; PR00906; SECA.
DR   SMART; SM00957; SecA_DEAD; 1.
DR   SMART; SM00958; SecA_PP_bind; 1.
DR   SUPFAM; SSF81767; SecA_PP_bd; 1.
DR   SUPFAM; SSF81886; SecA_SW; 1.
DR   TIGRFAMs; TIGR00963; SecA; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
DR   HOGENOMDNA; ECOBB_1.PE100; -.
KW   CAQ30615.1000068575old_1320000031;
KW   Protein translocase subunit secA ;
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Cytoplasm; Membrane; Metal-binding; Nucleotide-binding;
KW   Protein transport; Translocation; Transport; Zinc.
SQ   SEQUENCE   901 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLIKLLTKVF GSRNDRTLRR MRKVVNIINA MEPEMEKLSD EELKGKTAEF RARLEKGEVL
     ENLIPEAFAV VREASKRVFG MRHFDVQLLG GMVLNERCIA EMRTGEGKTL TATLPAYLNA
     LTGKGVHVVT VNDYLAQRDA ENNRPLFEFL GLTVGINLPG MPAPAKREAY AADITYGTNN
     EYGFDYLRDN MAFSPEERVQ RKLHYALVDE VDSILIDEAR TPLIISGPAE DSSEMYKRVN
     KIIPHLIRQE KEDSETFQGE GHFSVDEKSR QVNLTERGLV LIEELLVKEG IMDEGESLYS
     PANIMLMHHV TAALRAHALF TRDVDYIVKD GEVIIVDEHT GRTMQGRRWS DGLHQAVEAK
     EGVQIQNENQ TLASITFQNY FRLYEKLAGM TGTADTEAFE FSSIYKLDTV VVPTNRPMIR
     KDLPDLVYMT EAEKIQAIIE DIKERTAKGQ PVLVGTISIE KSELVSNELT KAGIKHNVLN
     AKFHANEAAI VAQAGYPAAV TIATNMAGRG TDIVLGGSWQ AEVAALENPT AEQIEKIKAD
     WQVRHDAVLE AGGLHIIGTE RHESRRIDNQ LRGRSGRQGD AGSSRFYLSM EDALMRIFAS
     DRVSGMMRKL GMKPGEAIEH PWVTKAIANA QRKVESRNFD IRKQLLEYDD VANDQRRAIY
     SQRNELLDVS DVSETINSIR EDVFKATIDA YIPPQSLEEM WDIPGLQERL KNDFDLDLPI
     AEWLDKEPEL HEETLRERIL AQSIEVYQRK EEVVGAEMMR HFEKGVMLQT LDSLWKEHLA
     AMDYLRQGIH LRGYAQKDPK QEYKRESFSM FAAMLESLKY EVISTLSKVQ VRMPEEVEEL
     EQQRRMEAER LAQMQQLSHQ DDDSAAAAAL AAQTGERKVG RNDPCPCGSG KKYKQCHGRL
     Q
//

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