(data stored in ACNUC7421 zone)

SWISSPROT: SECA_SHESH

ID   SECA_SHESH              Reviewed;         907 AA.
AC   A8FQA8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 70.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000255|HAMAP-Rule:MF_01382};
GN   OrderedLocusNames=Ssed_0418;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC       Note=May bind 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01382};
CC   -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}.
CC       Note=Distribution is 50-50. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
DR   EMBL; CP000821; ABV35031.1; -; Genomic_DNA.
DR   RefSeq; WP_012140768.1; NC_009831.1.
DR   ProteinModelPortal; A8FQA8; -.
DR   SMR; A8FQA8; -.
DR   STRING; 425104.Ssed_0418; -.
DR   EnsemblBacteria; ABV35031; ABV35031; Ssed_0418.
DR   KEGG; sse:Ssed_0418; -.
DR   eggNOG; ENOG4105CI6; Bacteria.
DR   eggNOG; COG0653; LUCA.
DR   HOGENOM; HOG000218168; -.
DR   KO; K03070; -.
DR   OMA; FEYDEVM; -.
DR   OrthoDB; POG091H01RS; -.
DR   Proteomes; UP000002015; Chromosome.
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   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
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   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; SSF52540; SSF52540; 3.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 2.
DR   TIGRFAMs; TIGR00963; secA; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQA8.
DR   SWISS-2DPAGE; A8FQA8.
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Cytoplasm; Membrane; Metal-binding; Nucleotide-binding;
KW   Protein transport; Translocation; Transport; Zinc.
FT   CHAIN         1    907       Protein translocase subunit SecA.
FT                                /FTId=PRO_1000087332.
FT   NP_BIND     102    109       ATP. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       891    891       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       893    893       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       902    902       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       903    903       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
SQ   SEQUENCE   907 AA;  102858 MW;  9A72A8E92785BF2B CRC64;
     MFGKILTKLF GSRNDRTLKS LGKTVTKINA LEDEYEKLTD EELKAKTTAF RGRLESGETL
     DDVMSEAFAV VREASKRVFE MRHFDVQMLG GMVLDSNRIA EMRTGEGKTL TATLPAYLNG
     LTGKGVHVIT VNDYLARRDA ENNRPLFEFL GLSVGINVAG LGQQEKKAAY DADITYGTNN
     EFGFDYLRDN MAFSPQERVQ RPLHYALIDE VDSILIDEAR TPLIISGAAE DSSELYTKIN
     TLIPHLVRQD KEDTEEEIGD GDYSIDEKAK QVHMTERGQE KVEVLLTERG MLAEGDSLYS
     AANISLLHHV NAALRAHTLF EKDVDYIVQD NEVIIVDEHT GRTMPGRRWS EGLHQAVEAK
     EGVHIQNENQ TLASITFQNF FRQYEKLAGM TGTADTEAFE FQHIYGLDTV VIPTNRPMVR
     KDHADLVYLT PDEKYAAIIE DIRGCRERGQ PVLVGTVSIE QSELLARLMK QEKIPHEVLN
     AKFHEREADI VAQAGRTGAV TIATNMAGRG TDIVLGGNWA MEIEVLTNPT DEQKAKIKTD
     WQVRHDEVVA AGGLHILGTE RHESRRIDNQ LRGRSGRQGD AGSSRFYLSM EDSLMRIFAS
     DRVSSMMKKL GMEKGEAIEH PWVSRAIENA QRKVEARNFD IRKQLLEFDD VANDQRQVVY
     AQRNELMDAE SIQDTIVNIQ ADVVNGLVDQ YIPQQSVEEL WDVPGLQTRL EQEYGLKMPV
     QEWLDKEDDL HEETLRERIV DTWVKSYQAK EEMVGEQVLR QFEKAVMLQT LDGLWKEHLA
     AMDHLRQGIH LRGYAQKNPK QEYKRESFEL FQQMLETLKH DVISVLSKVQ VQAQSDVEEM
     EERRRQEDAK IQRDYQHASA EAIVGAEEAE SLSAHTPVVR EGEKVGRNDP CPCGSGRKYK
     QCHGKLT
//

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