(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BI71_GEOS0

ID   A0A0F6BI71_GEOS0        Unreviewed;       791 AA.
AC   A0A0F6BI71;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 19.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
GN   Name=secA {ECO:0000256|HAMAP-Rule:MF_01382};
GN   OrderedLocusNames=GY4MC1_0274 {ECO:0000313|EMBL:ADP73122.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73122.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73122.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73122.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. Has a central role
CC       in coupling the hydrolysis of ATP to the transfer of proteins into
CC       and across the cell membrane, serving as an ATP-driven molecular
CC       motor driving the stepwise translocation of polypeptide chains
CC       across the membrane. {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01382}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01382}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01382}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_01382}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382}.
CC       Note=Distribution is 50-50. {ECO:0000256|HAMAP-Rule:MF_01382}.
CC   -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
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DR   EMBL; CP002293; ADP73122.1; -; Genomic_DNA.
DR   RefSeq; WP_013399911.1; NC_014650.1.
DR   EnsemblBacteria; ADP73122; ADP73122; GY4MC1_0274.
DR   KEGG; gmc:GY4MC1_0274; -.
DR   KO; K03070; -.
DR   OMA; IGQIHEF; -.
DR   OrthoDB; 212453at2; -.
DR   BioCyc; GSP581103:G1GOQ-317-MONOMER; -.
DR   Proteomes; UP000002034; 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: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   HAMAP; MF_01382; SecA; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000185; SecA.
DR   InterPro; IPR030908; SecA2_Bac_anthr.
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; 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   TIGRFAMs; TIGR04397; SecA2_Bac_anthr; 1.
DR   PROSITE; PS01312; SECA; 1.
DR   PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BI71.
DR   SWISS-2DPAGE; A0A0F6BI71.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874}.
FT   DOMAIN        1    570       SECA_MOTOR_DEAD. {ECO:0000259|PROSITE:
FT                                PS51196}.
FT   NP_BIND     100    107       ATP. {ECO:0000256|HAMAP-Rule:MF_01382}.
SQ   SEQUENCE   791 AA;  90448 MW;  053678B320D9E2BD CRC64;
     MLSYVKKLLN SDERRLKRYY KIVDHINALE PKFAKLSDQE LREKTAYFKN ELANGKTVFD
     IQAEAFAVVR EAAKRVLGMR HFDVQLIGGL VLAEGNIAEM ATGEGKTLVA SLPSYLRALE
     GKGVHVITVN EYLARRDREL IGQIHEFLGL TVGLNLPMME TEEKKAAYQA DITYGIGSEF
     GFDYLRDNMV YDISQRVQRP FHYAIIDEID SILIDEAKTP LIIAGKTGVS SELSYLCARI
     VKTLERDVDY YYDEETKATN LTEEGIAKIE RGFGIDNLYD VEHQTLYHYI IQALRAHVLF
     QRDVDYIVRD GKIVLIDMFT GRPMEGRSLS HGLHQAIEAK EGLELTEENK TQAAITIQNY
     FRLYPILSGM TGTAKTEEKE FQTLYGMDVV QIPTNKPVIR VDEPDRVFLT IDQKYKAVAK
     EVKRVHETGQ PVLIGTTSIL QSEKVAKYLE AENLPFRLLN AKTIEQEAQL IALAGQKGQI
     TIATNMAGRG TDIMLGEGVA ELGGLFVLGT ERHEARRIDN QLKGRAGRQG DPGRSQFFIS
     LEDDMFRRFA KEETEKWMKK AKTDENGEIL NKEIHEFVDR VQRICEGNSF SIREYNLKLD
     DVLNDQRTAV YRLRNRILEG DRLIPLVIDM LHSYVPYEIE QHCPADMLPE EWDLEKLTEQ
     LREIIPFPAV QLSGNINDIE DVKSNVQHSL EQYIHYLETM NDAEQVKAEI RPSLLSIVDY
     YWLNHLDAME RLKEGIGLRF YSQEDPIRQY QREGFELFVY MYHQIEADIC RRLAQAVAPK
     AAASESAGKT S
//

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