(data stored in ACNUC10821 zone)

SWISSPROT: SECA2_LISMF

ID   SECA2_LISMF             Reviewed;         776 AA.
AC   Q722W7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 86.
DE   RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382};
GN   OrderedLocusNames=LMOf2365_0612;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA   Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA   White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA   Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA   Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA   Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA   Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT   pathogen Listeria monocytogenes reveal new insights into the core genome
RT   components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC       the SecYEG preprotein conducting channel. Has a central role in
CC       coupling the hydrolysis of ATP to the transfer of proteins into and
CC       across the cell membrane, serving as an ATP-driven molecular motor
CC       driving the stepwise translocation of polypeptide chains across the
CC       membrane. {ECO:0000255|HAMAP-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. Other proteins may also be involved.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC       {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01382}.
DR   EMBL; AE017262; AAT03394.1; -; Genomic_DNA.
DR   RefSeq; WP_003725893.1; NC_002973.6.
DR   SMR; Q722W7; -.
DR   EnsemblBacteria; AAT03394; AAT03394; LMOf2365_0612.
DR   KEGG; lmf:LMOf2365_0612; -.
DR   HOGENOM; HOG000218169; -.
DR   KO; K03070; -.
DR   OMA; VNSSKIH; -.
DR   BioCyc; LMON265669:G1G0V-627-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-UniRule.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000185; SecA.
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   InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR   InterPro; IPR036670; SecA_X-link_sf.
DR   PANTHER; PTHR30612; PTHR30612; 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; 2.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q722W7.
DR   SWISS-2DPAGE; Q722W7.
KW   ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW   Protein transport; Translocation; Transport.
FT   CHAIN           1..776
FT                   /note="Protein translocase subunit SecA 2"
FT                   /id="PRO_0000318368"
FT   NP_BIND         95..102
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ   SEQUENCE   776 AA;  89436 MW;  47E13A75909C2C02 CRC64;
     MRQNYDDRKI VKQYREIARQ IVKKEGLYKN MDQAELCEQT NFWREKFKTK PMTDRDKINI
     FALAREAASR IIGLDAVVVQ LIGALVLGDG KVAEMKTGEG KTLMSLFVMF IEVMRGNRVH
     LVTANEYLAR RDREEIGQVL EYLGVSVALN ESGLDIAQKK AIYTADVIYG TASEFGFDYL
     RDNMVRQKED KVQSGLDFVL IDEADSILID EARTPLLISD RKEEDLSLYH TANKLVKKMM
     KDDYEMEEHK RFVWLNDAGI EKAQKFWGVE SLYSAEAQSE LRITMLLMRA HFLMHKDKDY
     VVLDDEVLII DPHTGRALPG RRFNDGLHQA IEAKEGVEVK EESRTLATIT IQNYFRMYKK
     ISGMTGTAKT EEEEFRQIYN MDVVVIPTNL RVNREDMQDD IFYTKKEKGR AIVYEVSWRY
     EKGQPTLIGT SSIKSNEWIS GLLDAAGIPH QVLNAKNHAQ EAEIIAKAGK RGMVTLATNM
     AGRGTDIKLD PDVHKLGGLA VIGTERHESR RIDLQLMGRS GRRGDPGFSK FMISLEDDLL
     EQFESKSWEK LSTKLKRKAP RDGKPVNSRK IHAVVVDAQK RLEGANYDIR KDLLSYDEVI
     DLQRKMVYKE RDLLLERNKL GVSSEKILRE VAEYSFIHPS DIPEEELEIY YSRQKELLGG
     TKFPISFDQV TLMDPREVVE EIVSWHKKER NKFPAETIAA IEREVYLNLM DQMWVMHLDA
     MVQLREGIHL RAYGQQDPLV MYQKEGAQLF EKFQADYHFY FAHALLELDP DGLIQG
//

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