SECA_LACH4
ID SECA_LACH4 Reviewed; 799 AA.
AC A8YUC4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=lhv_0720;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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}.
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DR EMBL; CP000517; ABX26862.1; -; Genomic_DNA.
DR RefSeq; WP_012211612.1; NC_010080.1.
DR AlphaFoldDB; A8YUC4; -.
DR SMR; A8YUC4; -.
DR STRING; 405566.lhv_0720; -.
DR EnsemblBacteria; ABX26862; ABX26862; lhv_0720.
DR KEGG; lhe:lhv_0720; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000790; 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; -; 3.
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; 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; TIGR00963; secA; 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; Translocase; Translocation; Transport.
FT CHAIN 1..799
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073480"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 799 AA; 91576 MW; 5C2FB12DC21F061E CRC64;
MLNILKKLYN DDKRELKKFE KYANKVEGYA DEMSKLTDEQ LQAKTPEFRE RIKKGESLDD
LLPEAFAVAR EGAKRVLGLY PFHVQILGGI ALHFGNIAEM MTGEGKTLTA TMPVYLNALE
GKGVHVVTVN EYLSSRDEEE MGQLYKWLGL TVGLNLNSMS PDEKREAYNC DVTYSTNSEL
GFDYLRDNMV VYKEQMVQRP LNYAIIDEVD SILIDEARTP LIISGEAEQA NSDYIRADRF
VKNLSEDKSD DDVDDDEDYG DYKIDWPTKT ISLTRTGIEK ACKHFGLRNL YDVENQKLVH
HIDQALRANY IMLKDIDYVV QDGEVLIVDS FTGRVMEGRR YSDGLHQAIE AKEGVKIQEE
SKTQATITYQ NFFRMYKKLS GMTGTAKTEE EEFREIYNMQ VITIPTNRPI ARKDMPDILY
PTLDSKFHAV VEEIKKRHAN GQPVLVGTVA IESSERLSHL LDEAGIPHAV LNAKNHAKEA
QIIMNAGQRG AVTIATNMAG RGTDIKLGPG VKELGGLAVI GTERHESRRI DNQLRGRSGR
QGDPGYTRFY LSLEDDLMKR FGGDRVKDFL DRLSDNDDDK VIESRLITRQ VESAQKRVEG
NNYDIRKQTL QYDDVMRIQR EIIYGERMQV IDADKSLKNV LIPMIHRTID SQVDMFTQGD
RSEWRLDSLR DFISSSLTSE QVTDSIDFKT ISVEDLKKKL YDIVEKNFED KEKALGDPSQ
MLEFEKVVIL RVVDDRWTDH IDAMDQLRQS IGLRGYGQLN PLVEYQDSGY RMFEEMISNI
EFDVTRLFMK AEIRQNISR
