ID Q722W7_LISMF PRELIMINARY; PRT; 776 AA. AC Q722W7; DT 05-JUL-2004 (TrEMBLrel. 27, Created) DT 05-JUL-2004 (TrEMBLrel. 27, Last sequence update) DT 05-JUL-2004 (TrEMBLrel. 27, Last annotation update) DE Preprotein translocase, SecA subunit, putative. GN OrderedLocusNames=LMOf2365_0612; OS Listeria monocytogenes (serotype 4b / strain F2365). OC Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=265669; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=15115801; DOI=10.1093/nar/gkh562; RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., RA Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., RA Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., RA Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., RA Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., RA Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., RA Bayles D.O., Luchansky J.B., Fraser C.M.; RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food- RT borne pathogen Listeria monocytogenes reveal new insights into the RT core genome components of this species."; RL Nucleic Acids Res. 32:2386-2395(2004). CC -!- FUNCTION: Involved in protein export. Interacts with the secY/secE CC subunits. SecA has a central role in coupling the hydrolysis of CC ATP to the transfer of pre-secretory periplasmic and outer CC membrane proteins across the membrane (By similarity). CC -!- SUBUNIT: Part of the prokaryotic protein translocation apparatus CC which comprise secA, secB, secD, secE, secF, secG and secY (By CC similarity). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017324; AAT03394.1; -; Genomic_DNA. DR TIGR; LMOf2365_0612; -. DR GO; GO:0016020; C:membrane; IEA. DR GO; GO:0005524; F:ATP binding; IEA. DR GO; GO:0004386; F:helicase activity; IEA. DR GO; GO:0003676; F:nucleic acid binding; IEA. DR GO; GO:0005515; F:protein binding; IEA. DR GO; GO:0017038; P:protein import; IEA. DR GO; GO:0006605; P:protein targeting; IEA. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR000185; SecA. DR InterPro; IPR011115; SecA_DEAD. DR InterPro; IPR011130; SecA_PP_bind. DR InterPro; IPR011116; SecA_SW. DR Pfam; PF00271; Helicase_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. KW ATP-binding; Complete proteome; DNA-binding; Hydrolase; Membrane; KW Protein transport; Translocation; Transport. 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 //