ID Q88YL7_LACPL PRELIMINARY; PRT; 787 AA. AC Q88YL7; DT 01-JUN-2003 (TrEMBLrel. 24, Created) DT 01-JUN-2003 (TrEMBLrel. 24, Last sequence update) DT 01-OCT-2003 (TrEMBLrel. 25, Last annotation update) DE Preprotein translocase, SecA subunit. GN Name=secA; OrderedLocusNames=lp_0739; OS Lactobacillus plantarum. OC Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=1590; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=NCIMB 8826 / WCFS1; RX MEDLINE=22480296; PubMed=12566566; DOI=10.1073/pnas.0337704100; RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., RA Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., RA Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., RA Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., RA De Vos W.M., Siezen R.J.; RT "Complete genome sequence of Lactobacillus plantarum WCFS1."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003). 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 -!- SUBCELLULAR LOCATION: Cytoplasmic side of membrane (By CC similarity). CC -!- SIMILARITY: Belongs to the secA family. 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; AL935254; CAD63334.1; -. DR HSSP; P28366; 1M6N. 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: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. DR TIGRFAMs; TIGR00963; secA; 1. DR PROSITE; PS01312; SECA; 1. KW ATP-binding; Complete proteome; Membrane; Protein transport; KW Translocation; Transport. SQ SEQUENCE 787 AA; 89558 MW; D97CE603A4294E50 CRC64; MANILKRWVE SDKRTIRRLD KIANKVEAYA DEYGKLSDAD LQAKTPEFRE RYKEGESLDD LLPEAFATAR EGAKRVLGLY PFHVQILGGI VLHQGDIAEM KTGEGKTLTA TMPVYLNAIS GKGVHVVTVN EYLSARDATE MGELYNWLGM SVGINGAEKS PEEKRAAYNA DITYSTNGEI GFDYLRDNMV VYREDMVQRP LNFAIIDEVD SILIDEARTP LIISGQSEGT TGMYKRADRF AKTLTKDEDY KVDLESKTVA LLDEGIRKAE KYFGLENLYD TDNTALNHYL DEALRANYIM LKDKDYVISD GQALIVDSFT GRIMDGRRFS DGLHQAIEAK EHVEIQEETK TMANITYQNL FRMYKKLSGM TGTAKTEQEE FREIYNMEVI TIPTNRPMIR DDRSDLLYPT LQSKFNAVVK EIKQLHEKGQ PMLIGTVAVE TSEYLSHRLD EENIPHVVLN AKNHAKEADI VANAGQRGAV TIATNMAGRG TDIKLGPGVK EVGGLAVIGT ERHESRRIDN QLRGRAGRQG DPGMSQFYLS LEDDLMLRFG SERIKNFLQR MNVEDDDAVI QSRMITRQVE SAQKRVEGNN YDSRKNVLQY DDVMRAQREV IYGERQQVIM EEKSLKPVIM PMIKRTVERT VQLHMQGDAK DWDLDAVVDF AQAAMVKEDS ISVADLKGKS PAEVEAYLMD RVDKIYADKA KQLYDAGQML EFEKVVILRV VDSHWTDHID AMDQLRQSIG LRGYGQLNPL VEYQRDGYQM FEEMVADIDY DTTRLFMKSE IRQNIQR //