ID   SECA_HERAR              Reviewed;         921 AA.
AC   A4G8S7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   10-AUG-2010, entry version 33.
DE   RecName: Full=Protein translocase subunit secA;
GN   Name=secA; OrderedLocusNames=HEAR2798;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M.,
RA   Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S.,
RA   Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier P.,
RA   Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D.,
RA   van Dorsselaer A., Weiss S., Weissenbach J., Lett M.-C., Danchin A.,
RA   Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-
RT   rich environments.";
RL   PLoS Genet. 3:518-530(2007).
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.
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DR   EMBL; CU207211; CAL62914.1; -; Genomic_DNA.
DR   RefSeq; YP_001101035.1; -.
DR   ProteinModelPortal; A4G8S7; -.
DR   SMR; A4G8S7; 7-845.
DR   STRING; A4G8S7; -.
DR   GeneID; 4931888; -.
DR   GenomeReviews; CU207211_GR; HEAR2798.
DR   KEGG; har:HEAR2798; -.
DR   NMPDR; fig|204773.3.peg.2666; -.
DR   eggNOG; COG0653; -.
DR   HOGENOM; HBG284200; -.
DR   OMA; GGMVLHD; -.
DR   PhylomeDB; A4G8S7; -.
DR   ProtClustDB; CLSK2516655; -.
DR   BioCyc; HARS204773:HEAR2798-MONOMER; -.
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:0005515; F:protein binding; IEA:InterPro.
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; IPR022491; SecA_preprotein_trnslcase.
DR   InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR   InterPro; IPR011116; SecA_Wing/Scaffold.
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   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.
PE   3: Inferred from homology;
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    921       Protein translocase subunit secA.
FT                                /FTId=PRO_0000320829.
FT   NP_BIND     100    107       ATP (Potential).
FT   METAL       905    905       Zinc (Potential).
FT   METAL       907    907       Zinc (Potential).
FT   METAL       916    916       Zinc (Potential).
FT   METAL       917    917       Zinc (Potential).
SQ   SEQUENCE   921 AA;  103427 MW;  263165E89E649367 CRC64;
     MSLLTQIFGS RNQRLLKQYQ KTVREINALE PAMEQLSDAA LQAKTPEFKE RLAKGEDIDS
     ILPEAFAVCR EASKRVLKMR HFDVQLIGGM TLHYGKIAEM GTGEGKTLMA TLPTYLNALT
     GKGVHVVTVN DYLAQRDAEW MGTLYGWLGL STGVNMSQID HDAKQIAYNS DITYGTNNEF
     GFDYLRDNMV YDTADRVQRD LHFAVVDEVD SILIDEARTP LIISGQAENH TELYHKINAV
     PPLLTLQIGE ETPDGKGTVE VPGDYTKDEK AHQVLLTEAG HEKAEQILTR MGLLPEGASL
     YDAANITLIH HLYAALRAHT LYHKDQHYVV QNDEVVIVDE FTGRLMTGRR WSDGLHQAVE
     AKEGVRIQNE NQTLASITFQ NYFRMYSKLA GMTGTADTEA YEFQEIYGLE TVVIPQNRPN
     QRKDRQDQVY KSSEEKYGAM LKDIQDCYER GQPVLVGTTS IENSELLSGI LNKANLPHNV
     LNAKQHAREA EIIAQAGRPK AITIATNMAG RGTDIVLGGN VAKQVQIIEA NDALSEAEKT
     AQAQKLGDEW QSLHDQVVAA GGLHIIGTER HESRRVDNQL RGRAGRQGDP GSSRFYLSLD
     DALLRIFAGD RVRAIMDRLK MPEGEPIEAG IVSRSIESAQ RKVEARNFDI RKQLLEYDDV
     ANDQRKVIYQ QRNELLETQD VSELITSLRQ GVFADLFRTY VPEQSMEEQW DLKALDEILR
     NEWQIDFSLA AVLEAEPNIT DEEMLERLLQ VTDAAYEAKV AIVGRESFAG FERGVMLQSV
     DSNWREHLAA LDHLRQGIHL RGYAQKNPKQ EYKREAFELF GQMLNLIKDA VVKTVMTVRI
     QSREEIDAAE EQLAQAHVEN VHYQHADFDP DAAPEELLAP TAQAHEAASQ PQVNTMPKVG
     RNDPCPCGSG KKYKQCHGRL A
//