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 02-JUN-2021, entry version 90. DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382}; DE EC=7.4.2.8 {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 -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + CC cellular protein(Side 2).; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP- CC 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}. 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; AE017262; AAT03394.1; -; Genomic_DNA. DR RefSeq; WP_003725893.1; NC_002973.6. DR SMR; Q722W7; -. DR KEGG; lmf:LMOf2365_0612; -. DR HOGENOM; CLU_005314_3_0_9; -. 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; KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding; KW Protein transport; Translocase; Translocation; Transport. FT CHAIN 1..776 FT /note="Protein translocase subunit SecA 2" FT /id="PRO_0000318368" FT NP_BIND 98..102 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 80 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382" FT BINDING 486 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 //