SECA_LACAC
ID SECA_LACAC Reviewed; 799 AA.
AC Q5FL75;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=LBA0673;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42549.1; -; Genomic_DNA.
DR RefSeq; WP_011254222.1; NC_006814.3.
DR RefSeq; YP_193580.1; NC_006814.3.
DR AlphaFoldDB; Q5FL75; -.
DR SMR; Q5FL75; -.
DR STRING; 272621.LBA0673; -.
DR PRIDE; Q5FL75; -.
DR EnsemblBacteria; AAV42549; AAV42549; LBA0673.
DR GeneID; 56942305; -.
DR KEGG; lac:LBA0673; -.
DR PATRIC; fig|272621.13.peg.643; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; MVHYDVQ; -.
DR BioCyc; LACI272621:G1G49-695-MON; -.
DR Proteomes; UP000006381; 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; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..799
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000073475"
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; 91555 MW; 1AD9451DB39D2CC1 CRC64;
MANILKKLYN TDKRELKKFE KYATKVEEHA DEMSKLSDEQ LQAKTPEFRE RIKNGESLDD
LLPEAFAVAR EGAKRVLGLY PFHVQILGGI ALHFGNIAEM MTGEGKTLTA TMPVYLNALE
GKGVHVVTVN EYLSSRDEEE MGQLYRWLGL TVGLNINSMS PDEKREAYNC DVTYSTNSEL
GFDYLRDNMV VYKEQMVQRP LNYAIIDEVD SILIDEARTP LIISGEAEQA NSDYIRADRF
VKTLTEDKSD DDADDDEDHG DYKIDWPTKT ISLTRTGIEK ACEHFGLKNL YDVENQKLVH
HIDQALRANY IMLKDIDYVV QDGEVLIVDS FTGRVMEGRR YSDGLHQAIE AKEGVKIQEE
SRTQATITYQ NFFRMYKKLS GMTGTGKTEE EEFREIYNMQ VITIPTNRPI ARKDMPDILY
PTLDSKFHAV IEEIKKRHAK GQPVLVGTVA IESSERLSHL LDEANIPHAV LNAKNHAKEA
QIIMNAGQRG AVTIATNMAG RGTDIKLGPG VKELGGLAVI GTERHESRRI DNQLRGRSGR
QGDPGYTRFY LSLEDDLMKR FGGDRVKDFL DRLSDNDDEK VIESRLITRQ VESAQKRVEG
NNYDTRKQTL QYDDVMRIQR EIIYGERMQV IEADKSLKNV LIPMIHRTIN SQVDMFTQGD
RSQWRLDSLR DFISSSLASE QVTDSIDFKT ISVEDLKKKL YDIVEKNFED KEKALGDPSQ
MLEFEKVVIL RVVDDRWTDH IDAMDQLRQS IGLRGYGQLN PLVEYQDSGY RMFEEMISNI
EFDVTRLFMK AEIRQNLSR
