SECA_AMOA5
ID SECA_AMOA5 Reviewed; 1116 AA.
AC B3ESI0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Aasi_0806;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01382}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}.
CC Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-
CC 50. {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; CP001102; ACE06182.1; -; Genomic_DNA.
DR RefSeq; WP_012472951.1; NC_010830.1.
DR AlphaFoldDB; B3ESI0; -.
DR SMR; B3ESI0; -.
DR STRING; 452471.Aasi_0806; -.
DR EnsemblBacteria; ACE06182; ACE06182; Aasi_0806.
DR KEGG; aas:Aasi_0806; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_0_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000001227; 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 PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..1116
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000144972"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 194..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 693
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1116 AA; 128236 MW; 935B313D9B1982DA CRC64;
MLKLFTKLFG TKSERDLKSI RPYVEKINLE YEKLVSLTND ELRKKTDSLK QYIKVETQEF
IGELEIRERQ LEATTQLTPK EVEDLYIQIS RIKEQYNTQL EKVLLDILPQ AFAIVKETAR
RFKENEQLIV TATGYDRELA ITEKHIDIEG DQAIWKNQWE VTGHLLTWDM VHYDEQLIGG
VILHKGKIAE MATGEGKTLV ATLPTFLNAL VGKGVHIVTV NEYLAKRDAA WMKPIYQFHG
FTVACIEETS PYSAARREAY QADITYGTNN EFGFDYLRDN MASQQEEVVQ REHHYAIVDE
VDSVLIDDAR TPLIISGPVE KGNEQEYITF NPRIKRLYEA QKQIVNQFLQ EAKSQMVAGK
NDEAGLPLFR AYRGLPKYKP LIKYLSEPGV KQLLHKTENY YIQDNSRMMP EADEPLLFTI
DEKHNTVELT EKGLEYITQQ GEDPDFFILP DTATAVGEIE SDAGLDNLEK EQKKQILAQE
YAIKSQRIHA VQQLLKAYAL FEKDIDYILV DGKAKIVDEQ TGRVLEGRRY SDGLHQAIEA
KEEIKIEKAS QTYATITLQN YFRLYHKLAG MTGTAETEAG EFYDIYHLDV VVTPTHKPVV
REDKDDKVYK TVREKFNAII EEITVLANQG RPVLVGTTSV EISELVSKML NLRKIKHQVL
NAKHHQKEAE IVAEAGKPGT VTIATNMAGR GTDIKLSPEA KAAGGLAIIG TERHESRRVD
RQLRGRAGRQ GDVGSSQFFV SLEDSLMRLF ISDRIAKIMD SLGLKEGEMI QHSMITRSIE
RAQKKVEQNN YAYRKRLLEY DNELNKQREI IYRRRRDALL GHRLGAEVNA MLFEVAKSSV
MQQGVKANYH VLATKFSYIT GTLPPITEEE FHTYDIQKIT DIIYQAFLSS YMNRLAVFKE
QGIAVQMNLP DHIADIRAEY LSFSFSDSER RLEVPVKIAD FMDNAGEAIL KSLERVAIIY
YLDRYWQEHL RYMDELRHSV QNASYEQKDP LLIYKFESYA LFSTMIARAN ESIITYLLKA
NLLLYKASDE KPKMVEKNKR IELEESKQDI ISLLRERASN SSEEILKPQP IKSQKIANRN
ERVTVQYEDG TIKENVKFKS VEEDIANGKC ILLETR
