(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE1034

ID   ACAM1_1_PE1034                       STANDARD;      PRT;   929 AA.
AC   ACAM1_1_PE1034; B0C1V9;
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; (ACAM1_1.PE1034).
GN   Name=secA; OrderedLocusNames=AM1_1087;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_1.PE1034.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:SECA_ACAM1
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 as an ATP-driven molecular
CC       motor driving the stepwise translocation of polypeptide chains
CC       across the membrane (By similarity).
CC   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in
CC       cyanobacterial cells (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 SecDF. Other proteins may also
CC       be involved (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Cellular thylakoid
CC       membrane; Peripheral membrane protein; Cytoplasmic side
CC       (Potential). Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the SecA family.
CC   -!- GENE_FAMILY: HOG000218168 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0C1V9; -.
DR   EMBL; CP000828; ABW26125.1; -; Genomic_DNA.
DR   RefSeq; YP_001515439.1; NC_009925.1.
DR   ProteinModelPortal; B0C1V9; -.
DR   SMR; B0C1V9; 10-230.
DR   STRING; B0C1V9; -.
DR   GeneID; 5679911; -.
DR   GenomeReviews; CP000828_GR; AM1_1087.
DR   KEGG; amr:AM1_1087; -.
DR   OMA; GGMVLHD; -.
DR   ProtClustDB; PRK12902; -.
DR   BioCyc; AMAR329726:AM1_1087-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP 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; 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; 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; ACAM1_1.PE1034; -.
KW   preprotein translocase subunit SecA;
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Cytoplasm; Membrane; Nucleotide-binding; Protein transport; Thylakoid;
KW   Translocation; Transport.
SQ   SEQUENCE   929 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLKTLLGDPN KRKLKKYQPD VVEINLLEEE VEVLSDQELR AKTDEFKERL KNGETLDDLL
     PETFAVVREA SKRVLGMRHF DVQLLGGMIL HDGQIAEMKT GEGKTLVSTL PAYLNALTGK
     GVHAITVNDY LARRDAEWMG QVHRFLGLSV GLIQQSMSPT ERKKNYACDI TYGTNSEIGF
     DYLRDNMSTS IEEVVQRPLN YCVIDEVDSV LIDEARTPLI ISGQVERPTE KYLDASKVAN
     ALQPEEHYEV DEKARNVILT DEGFVEAEKI LGVSDLFDPE DPWAHYVFNA IKAKELFIND
     VNYIVRNDEI VIVDEFTGRV MPGRRWSDGL HQAIEAKEKV EIQNETQTLA TITYQNLFLL
     YDKLAGMTGT AKTEEAEFEK IYKLEVTIVP TNRSNQRQDI SDVVYKSEEA KWLAVANECA
     DMYEVGRPIL VGTTSVEKSE VLSKLLLERN IPHNLLNAKP ENVERESEIV AQAGREGRVT
     IATNMAGRGT DIILGGNAEY MARLKVREYL MPRIVQPEDD NPLSMMQVKL PEAGSQGFGG
     DGQQKGMQRK TWKVSPEIFP TTISKDAESL LKEAVNAAVK QYGEQSLPEL QAEDLMAVAS
     EKAPTDDPVI QKLREVYNLI LEEYEAFTSK EHDKVVERGG LHVIGTERHD SRRIDNQLRG
     RAGRQGDPGS TRFFLSLQDN LLRIFGGDRV AGLMNAFRVE EDMPIESRIL TSSLENAQKK
     VETYYYDIRK QVFEYDEVMN NQRRAIYAER RRVLEGEDLK ERVIEYAEQT MDDIVEAYVN
     PELPPEEWNL EQLVDKTKEF VYLLEDLEAS HIADLSMPEM KMFLREQVRI AYDQKESEVN
     EMEPTLMRQA ERFFILQQID MLWREHLQQM DALREAVGLR GYGQQDPLIE YKSEGYEVFL
     DMMTAIRRNV VYSLFQFRPQ RQPEPSEVA
//

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