SECA2_LACJO
ID SECA2_LACJO Reviewed; 788 AA.
AC Q74L37;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 126.
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}; OrderedLocusNames=LJ_0388;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(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 + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 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; AE017198; AAS08378.1; -; Genomic_DNA.
DR RefSeq; WP_011161547.1; NC_005362.1.
DR AlphaFoldDB; Q74L37; -.
DR SMR; Q74L37; -.
DR STRING; 257314.LJ_0388; -.
DR PRIDE; Q74L37; -.
DR EnsemblBacteria; AAS08378; AAS08378; LJ_0388.
DR KEGG; ljo:LJ_0388; -.
DR PATRIC; fig|257314.6.peg.410; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR Proteomes; UP000000581; Chromosome.
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:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
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 CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR022490; SecA2.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
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 TIGRFAMs; TIGR03714; secA2; 1.
DR PROSITE; PS01312; SECA; 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; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..788
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318363"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 95..99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 788 AA; 89385 MW; 933E0885E4E2DB10 CRC64;
MLTDRLRLKK ARKLLNKINK LGPKMQAMSD EKLQGQTAIF KKQLKEGKSL DDILPEAYAT
VREADKRILG MFPYDVQVLG AIVLHNGSIA EMKTGEGKTL VATMALYLNA LEGKGAMLVT
PNGYLASRDK KELAPVYEWL GLSVSLAFAE EKDSKKKITA KTKRKWYNSD IVYTTASSLA
FDYLFNNLAS SKENQYLRPF NYVIVDEVDE VLLDEAQTPF VVSSSPNVQS NLYHLADQFV
RLLDPEVDYV FKKDDQLFWL TAHGIEKAEQ FFKLDSLFSN ESRSVYRHII LAMGAHLTMR
RGHDYLVVKG EVVLLDEDSG RLKRGVQVST GIHQAVEAKE KVELTKIQKT AASITFPALF
ALFNKVSGMS GTAKVNEEEF LQTYNLKVVT IPTRVPVIRK DYRPLIFLTT IDKLMTAVDD
VVEMHKTGRP VLLVAGSVEN SEIISELLLN IGIPHNVLNA YNAAYEAQII KNAGQKNAVT
IATNMAGRGT DIKLGPGVKE LGGLAVIGTE MLPKRVELQL AGRAGRQGDP GSSQFLISLE
DSFISSNNTP RQKKYYRKLM KKKSKGKDIT LLSGPRIRFS LLMLRTRKED LNELMRSQTN
KMEIILSLQR KNFYTRRDKI MKTDDLQEDV DRIIDNALNL YLEKQDLSNK SDLKYFINQH
VTYQQVNVPD NLKTKKAIKD FLKELAYKIL DEKKHVLINK KQANDFYQQV IISSMDGNWI
DQVDRIEKIK INAQQWGRSG RPQDLLHQEK AFEAYKDFLD KITLSTFDNL LLSKIFTNEK
GQLVVVFN
