(data stored in ACNUC7421 zone)

HOGENOM: OCHA4_1_PE1010

ID   OCHA4_1_PE1010                       STANDARD;      PRT;   906 AA.
AC   OCHA4_1_PE1010; A6WXN8;
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; (OCHA4_1.PE1010).
GN   Name=secA; OrderedLocusNames=Oant_1021;
OS   OCHROBACTRUM ANTHROPI ATCC 49188.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae;
OC   Ochrobactrum.
OX   NCBI_TaxID=439375;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS OCHA4_1.PE1010.
CC       Ochrobactrum anthropi ATCC 49188 chromosome 1, complete sequence.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:SECA_OCHA4
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 (Potential).
CC   -!- SUBUNIT: Monomer and homodimer (By similarity). Part of the
CC       essential Sec protein translocation apparatus which comprises
CC       SecA, SecYEG and auxiliary proteins SecDFyajC and YidC(OxaA) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Cytoplasm (By
CC       similarity). Note=Distribution is 50-50 (By similarity).
CC   -!- SIMILARITY: Belongs to the SecA family.
CC   -!- GENE_FAMILY: HOG000218168 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A6WXN8; -.
DR   EMBL; CP000758; ABS13742.1; -; Genomic_DNA.
DR   RefSeq; YP_001369571.1; NC_009667.1.
DR   ProteinModelPortal; A6WXN8; -.
DR   SMR; A6WXN8; 16-236.
DR   STRING; A6WXN8; -.
DR   GeneID; 5380992; -.
DR   GenomeReviews; CP000758_GR; Oant_1021.
DR   KEGG; oan:Oant_1021; -.
DR   eggNOG; COG0653; -.
DR   OMA; GGMVLHD; -.
DR   ProtClustDB; PRK12904; -.
DR   BioCyc; OANT439375:OANT_1021-MON; -.
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:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
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; OCHA4_1.PE1010; -.
KW   preprotein 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   906 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVSFGGFARK IFGSSNDRRV KTLRQRANQI TAIEKNYENL TDEQLQAKTA EFRAALAGGK
     TLDSLLPDAF ATAREAAKRV LGMRPFDVQL IGGMVLHERG IAEMRTGEGK TLMATLPVYL
     NALEGKGVHV VTVNDYLATR DAETMGKLYN FLGLTVGVIK HGLDDDERRA AYACDITYGT
     NNELGFDYLR DNMKYERAQM VQRPHNYAIV DEVDSILIDE ARTPLIISGP LEDRSDFYNL
     IDTFIPALEP EDFEIDEKQK TAIFTEVGTE KVEQLLEAAG HLKGESLYDI ENVAVVHHLN
     NALRAHKLFQ RDKDYIVRND EIVIIDEFTG RMMPGRRYSE GLHQALEAKE HVTIQPENQT
     LASITFQNYF RMYNKLSGMT GTAATEAEEF GNIYGLEVLE IPTNLPVQRI DEDDEVYRSV
     EEKYRAIVRD IRASHEKGQP ILVGTTSIEK SEQLAERLRK EGIKEFQVLN ARYHEQEAYI
     IAQAGVPGTV TIATNMAGRG TDIQLGGNLE MRVRQELSDI PEGPERDAKI AEIKADIAQL
     KEKALAAGGL YVLATERHES RRIDNQLRGR SGRQGDPGRS KFFLSLQDDL MRIFGSDRMD
     SMLQKLGLKE DEAIVHPWIN KALEKAQKKV EARNFEIRKN LLKYDDVMND QRKVIFEQRL
     EMMDEEDLTE TVGEMRHEVI EDMVALRIPK DAYAEKWDIA GLKEDIISKL NLDLPVEDWA
     KEEGIAEEEF ENRIKEAADK AAAEKAERFG PQIMTYVEKS VIMQSLDNLW REHLVNLDHL
     RSVVGFRGYA QRDPLNEYKT EAFELFQSML ANLREVVISQ LMRVEIVREA PPEPELPPMT
     GRHIDSTTGE NDFDEASWSD HQHDERNVPA AERDPADPRT WGKVSRNEAC PCGSGKKYKH
     CHGAFE
//

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