SECA_GRAFK
ID SECA_GRAFK Reviewed; 1119 AA.
AC A0LYR8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=GFO_0530;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL65513.1; -; Genomic_DNA.
DR RefSeq; WP_011708451.1; NC_008571.1.
DR AlphaFoldDB; A0LYR8; -.
DR SMR; A0LYR8; -.
DR STRING; 411154.GFO_0530; -.
DR EnsemblBacteria; CAL65513; CAL65513; GFO_0530.
DR KEGG; gfo:GFO_0530; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000755; 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 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 inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Protein transport; Translocase; Translocation;
KW Transport.
FT CHAIN 1..1119
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320821"
FT REGION 1025..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 195..199
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1119 AA; 127561 MW; 773D8344A058610A CRC64;
MSFLDSVLKA FVGDKSKKDV KEIQPIVNKI KALESEFEAL SLDELRAKTS EFKAKIAEAT
KEVEDKIVAL NKEADEIDDI TRKEDIYAEV DALKEKSYEI SEAVLNDILP EAFATVKETA
KRFVNNTQLK VKASSFDREI SAEKDYVTLE DDHAIWSNSW DAAGKPVTWD MVHYDVQLIG
GVAMHQGKIA EMQTGEGKTL VATLPMYLNA LTGNGVHLVT VNDYLAKRDS AWMAPIFQFH
GMSVDCVDYH RPNSAARRKA YNADITYGTN NEFGFDYLRD NMSHAPDDLV QRPHNYAIVD
EVDSVLVDDA RTPLIISGPV PKGDTHEFME LKPAIANIVE VQRKHLVKVL SEAKKLIKEG
DTKEGGFQLL RVYRGLPKNK ALIKFLSEEG IKQLLQKTEN HYMQDNNREM PKVDAELYFT
IEEKSNQIDL TDKGIEFLSG KDEPDFFVMP EIGMEIAKIE KEGFPAEEEA EKKEELFRDY
SVKSERIHTL RQLLKSYTLF EKDTEYVVID NKVKIVDEQT GRIMEGRRYS DGLHQAIEAK
ENVKIEDATQ TFATVTLQNY FRMYGKLSGM TGTAVTEAGE LWEIYKLDVV EIPTNRPIAR
NDKEDLVYKT KREKYNAVID HVTDLSNAGR PVLIGTTSVE ISELLSRMLK LRNVPHNVLN
AKRHKQEADI VAEAGNSGIV TIATNMAGRG TDIKLSKEVK EAGGLAIVGT ERHDSRRVDR
QLRGRAGRQG DPGSSQFYVS LEDNLMRLFG SERIAKLMDR MGLEEGEVIQ HSMISKSIER
AQKKVEENNF GVRKRLLEYD DVMNAQREVI YKRRYHALFG ERLRVDLANM IFDISESITE
TNKAAEDFKN FEFELIRNFS MSSPVSEEEF KKMNAQKLAG EVYKSAYKHY DEKMSHNAER
AFPVIKQVHE DERNNFERIS VPFTDGTKTL SVVTNLEKAY ETEGKQLIKD FEKNITLAII
DDAWKTHLRK MDELKQSVQL AVHEQKDPLL IYKFEAFELF KVMLENVNRD VMSFLFKGEI
PSTGAPSIHE ARQTKSKEKV ETRKEEIPNM DERAAQSRAA GNTQRQQPEV TETIVRDRPK
IGRNDKVTVK NVMSGESKTM KFKQAIPLLD KGDWVLVEE
