SECA_WIGBR
ID SECA_WIGBR Reviewed; 832 AA.
AC Q8D301;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=WIGBR2000;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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:0000250}.
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-YajC and YidC. {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, ECO:0000305}.
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DR EMBL; BA000021; BAC24346.1; -; Genomic_DNA.
DR RefSeq; WP_011070004.1; NC_004344.2.
DR AlphaFoldDB; Q8D301; -.
DR SMR; Q8D301; -.
DR STRING; 36870.25166155; -.
DR PRIDE; Q8D301; -.
DR EnsemblBacteria; BAC24346; BAC24346; BAC24346.
DR KEGG; wbr:secA; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_6; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000562; 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; 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..832
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321038"
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 512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 832 AA; 96372 MW; 547307B66B7AC157 CRC64;
MLIKLFGKIF KNSNDRALKV INLIVKKINS LESTIEKLTD QQLSSKTIEF KNRISDGDNL
NNILPEAYAV VREASKRIFN MRHFDVQLMG GIVLNRRCIA EMSTGEGKTL TSVLPAYLHS
LLGKGVHIVT VNDYLAKRDA NNNKPLFEFL GITVGINLPG LNNIEKRNAY LADITYGTNN
EYGFDYLRDN MIFNENEKVQ RNLYFALVDE VDSILIDESR TPLIISGPIK SNSDIYYKIN
KLVPNLIKQE KEDSENFQGN GHFTIDEKSK QINMTERGLI LVENLLIKNH LMNKNDSLYS
SKNISLMHHF ISALRAHKLF FKNVDYIVKN NEIIIVDEHT GRTMHGRRWS DGLHQAIEAK
EKVNINNENQ TLASITFQNY FRLYEKLSGM TGTAYTEAAE FKAIYKLDTI IIPTNRPVIR
NDLPDLIYMT EKEKINAIIN DIKNCYSKNI PVLVGTISIE KSENISNILK KLRIKHNVLN
AKFHELEAEI ISQAGCPKSI TIATNMAGRG TDIILGGNWK SEFFNKKNIN KKRIKKIKES
WVKKNNYVIK LGGLHIIGTE RHESRRIDNQ LRGRSGRQGD PGSSRFYVSM EDNLMRIFAS
NRIIQTMQKL GMKTGESIEH KWITKAISNA QKKVENRNFD MRKQLLDYDD VANEQRKAIY
SQRTEILNSL DIKDIIDNIR KDVLKKIFEK YKTKHSEKIN VNLIKIENLI KKYFCIEISI
LSLYKENKCN LEKLYKNILI IILKKYNEKE NKIGSTNLRI FEKNIMIKTL DSFWREHLSS
IDYLRQGIHL RGYAQKDPKQ EYKRESFIMF ENMLYELKIE VITIISNVKI KS
