SECA_NOCFA
ID SECA_NOCFA Reviewed; 937 AA.
AC Q5YQU1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=NFA_45990;
OS Nocardia farcinica (strain IFM 10152).
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX NCBI_TaxID=247156;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFM 10152;
RX PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA Shiba T., Hattori M.;
RT "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(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}.
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DR EMBL; AP006618; BAD59450.1; -; Genomic_DNA.
DR RefSeq; WP_011211134.1; NC_006361.1.
DR AlphaFoldDB; Q5YQU1; -.
DR SMR; Q5YQU1; -.
DR STRING; 247156.NFA_45990; -.
DR EnsemblBacteria; BAD59450; BAD59450; NFA_45990.
DR GeneID; 61135204; -.
DR KEGG; nfa:NFA_45990; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_11; -.
DR OMA; MVHYDVQ; -.
DR BioCyc; NFAR247156:NFA_RS22810-MON; -.
DR Proteomes; UP000006820; 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; 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..937
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000318398"
FT REGION 881..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 105..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 494
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 937 AA; 104253 MW; D2DB73373D689838 CRC64;
MPALTLTRLL RIGEGRTVKR LAHLADEVLA LGSDYEQLTD AELRAKTDEF KQRYADGETL
DDLLLEAFAV AREASWRVLN QKHYKVQVMG GAALHLGNIA EMKTGEGKTL TCVLPAYLNA
LSGDGVHVVT VNDYLAKRDA EWMGRVHRFL GLEVGVILGG MTPPQRRVAY AADITYGTNN
EFGFDYLRDN MAHSLDDLVQ RGHNFAVVDE VDSILIDEAR TPLIISGPAD ASSKWYAEFA
RIAPLLKKDV HYEVDIKKRT IGVHEAGVEF VEDQLGIDNL YEAANSPLVS YLNNAIKAKE
LYQRDKDYIV RDGEVIIVDE FTGRILVGRR YNEGMHQAIE AKEGVEIQPE NQTLATITLQ
NYFRLYDKLS GMTGTAETEA AELHQIYNLG VVPIPTNKPM IRVDQSDLIY KTEEAKFNAV
VDDVAERHEK GQPVLIGTTS VERSEYLSKQ FTRRGIPHSV LNAKFHEQEA QIIAEAGRPG
AVTVATNMAG RGTDIVLGGN PDIIADILLR KQGLDPVETP EEYEAAWLPT LEQVKAQTAA
DADAVREAGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSLGDE LMRRFNGAAL
EAIMTRLNLP DDVPIEAKMV SKAIKSAQTQ VEQQNFEIRK NVLKYDEVMN QQRTVIYGER
NRILRGEDME GQVQNMITDV ITAYVDGATA EGYVEDWDLE KLWTALKTLY PVSLDYRELT
GELDGEPRDL SREELREALL EDAHSAYAKR EQEIDGLAGE GSMRNLERQV LLSVLDRKWR
EHLYEMDYLK EGIGLRAMAQ RDPLVEYQRE GFDMFTAMLD GLKEESVGFL FNLQVEVQQP
QPTGVSVDPG LRSPVGATVP APAPAAPTPL LAKGITDQAP RGLNYIGPDE GGRASVHSDA
EEYGGGTPAA AGTRRERREA ARAEGKGKRG PKSRRKH
