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SECA_BEUC1
ID   SECA_BEUC1              Reviewed;         968 AA.
AC   C5C1N8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Bcav_1246;
OS   Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC   Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; Beutenbergia.
OX   NCBI_TaxID=471853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX   PubMed=21304633; DOI=10.4056/sigs.1162;
RA   Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA   Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA   Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT   0122).";
RL   Stand. Genomic Sci. 1:21-28(2009).
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; CP001618; ACQ79506.1; -; Genomic_DNA.
DR   RefSeq; WP_015881746.1; NC_012669.1.
DR   AlphaFoldDB; C5C1N8; -.
DR   SMR; C5C1N8; -.
DR   STRING; 471853.Bcav_1246; -.
DR   PRIDE; C5C1N8; -.
DR   EnsemblBacteria; ACQ79506; ACQ79506; Bcav_1246.
DR   KEGG; bcv:Bcav_1246; -.
DR   eggNOG; COG0653; Bacteria.
DR   HOGENOM; CLU_005314_3_0_11; -.
DR   OMA; MVHYDVQ; -.
DR   OrthoDB; 212453at2; -.
DR   Proteomes; UP000007962; 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..968
FT                   /note="Protein translocase subunit SecA"
FT                   /id="PRO_1000215100"
FT   REGION          835..968
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT   BINDING         104..108
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   968 AA;  106061 MW;  F1A61A9FB51C9781 CRC64;
     MPSILDKVLR MGEGRILKKL TGIVAQVNAH EDTVREFTDA ELREETDVFK ARLADGETLE
     AILPEAFATV REAARRTLGQ RPHDVQVMGG AALHLGNIAE MKTGEGKTLA ATLPAYLNAL
     SGDGVHVVTV NDYLAQYQSD LMGRVYRFLG LTTGCILSGQ KPEERRRHYA ADITYGTNNE
     LGFDYLRDNM AWSSGELVQR GHNFVIVDEV DSILIDEART PLIISGPASG DANKWYAEFA
     RVARRLTRES DYEVDEKKRN VGVLEPGIEK VEDYLGIDNL YESLNTPLIG FLNNAIKAKE
     LFKRDKDYVV LKGEVLIVDE HTGRILAGRR YNEGMHQAIE AKEGVAIKAE NQTLATITLQ
     NYFRLYGKLA GMTGTAMTEA AEFQGTYKVG VVPIPTNMPM ARLDKPDLVF KNEDGKFDAV
     VEDIVERHAA GQPVLVGTTS VEKSELLSTK LKRQGVPHEV LNAKQHAREA SIVAMAGRKG
     AVTVATNMAG RGTDIMLGGN AEHLAIATLA EQGLDPNETP EEYEAAWPDA LEEATTSVAA
     EHDEVVDLGG LYVLGTERHE SRRIDNQLRG RSGRQGDPGE SRFYLSMGDD LMRLFNSGLA
     ERFMGSSAYP DDMPLESKLV TRGIASAQGQ VEARNFEIRK NVLKYDDVLS RQRAVIYTDR
     RRVLEGEDLA EQVQGFLTDV VTAYIESATQ AGAPESWDLD ELWTALKAVY PISITPEEVV
     SEAGNATRVT PEMLTREILS DAEHAYARRE EELTPDVMRQ LERRVVLAVL DRKWREHLYE
     MDYLKEGIGL RAMAQRDPLV EYQREGFQLF SAMRDAIKEE AVGYLFNLEV KRPEPAESAE
     ESTDGAPVVP AVPTGSDGEP LAPEQEAVPA GEPERPAKRR PAARVATRPA AEVDPLGLDT
     PERPAALQYS APSSDGGSSF SEGRVVRSEG GTSGGSARPA AGASSGGGGG GANREARRRA
     AKAAKKRR
 
 
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