SECA_BRAHW
ID SECA_BRAHW Reviewed; 980 AA.
AC C0QZS7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=BHWA1_00872;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND BIOTECHNOLOGY.
RX PubMed=19179021; DOI=10.1016/j.vetmic.2008.12.018;
RA Song Y., La T., Phillips N.D., Bellgard M.I., Hampson D.J.;
RT "A reverse vaccinology approach to swine dysentery vaccine development.";
RL Vet. Microbiol. 137:111-119(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC Note=May bind 1 zinc ion per subunit. {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 -!- BIOTECHNOLOGY: Has shown promise in a 4-component vaccine with
CC BHWA1_00430 (AC C0QY54), BHWA1_00569 (AC C0QYX7) and flaAL (AC C0QWY9).
CC {ECO:0000269|PubMed:19179021}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; EU555159; ACD74829.1; -; Genomic_DNA.
DR EMBL; CP001357; ACN83365.1; -; Genomic_DNA.
DR RefSeq; WP_012670414.1; NC_012225.1.
DR AlphaFoldDB; C0QZS7; -.
DR SMR; C0QZS7; -.
DR STRING; 565034.BHWA1_00872; -.
DR EnsemblBacteria; ACN83365; ACN83365; BHWA1_00872.
DR GeneID; 63961982; -.
DR KEGG; bhy:BHWA1_00872; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_12; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000001803; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR004027; SEC_C_motif.
DR InterPro; IPR000185; SecA.
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; PF02810; SEC-C; 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; PS51196; SECA_MOTOR_DEAD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleotide-binding; Protein transport; Translocase;
KW Translocation; Transport; Zinc.
FT CHAIN 1..980
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000184216"
FT REGION 954..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 127..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 529
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 962
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 964
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 973
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 974
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 980 AA; 111045 MW; C84794027862926E CRC64;
MGAMDLVFKL IFGSKEQNDA KILKPIAEKT LTFEEEIKKL SNEELTNKTK EFRERVEKYI
GCKTEELDLS KEENKKKLQN ILDEILPEAF AVVREASIRT TGMRHFDVQV MGGAVLHQGR
IAEMKTGEGK TLVATLAVYL NALTGLGVHV VTVNDYLAKR DAEWMTPIYS MLGISVGILD
NTRPHSPERR AVYNCDVVYG TNNEFGFDYL RDNMVTRKED KVQRKFYFAI VDEVDSILID
EARTPLIISG PAEKNIKMYY EIDRIIPMLK QAEVDERMRE VAGTGDYVLD EKDKNVYLTE
EGVHKVEKLL NVENLYGAQS STIVHHVNQA LKAHKVFKKD VDYMVTDGEV LIVDEFTGRV
LEGRRYSDGL HQAIEAKEKV AIQNESQTYA TITFQNYFRM YPKLSGMTGT AETEAEEFYK
IYKLDVAVIP TNKPIARQDL SDRIYRTRKA KFEALAKYIK ELQDAGKPAL VGTVSVEMNE
ELSKVFKRHK INHEVLNAKN HSREAAIIAQ AGEPGAVTLA TNMAGRGTDI VLGGNPVAKG
VAEIEQILVL MRDKAFKERD PYKKEELTKK IKSIDLYKEA FVRSVISGKI EEAKELAQKN
NADEMIEKID RIIQINEKAK VDKERVLAAG GLHVIGSERH EARRIDNQLR GRSGRQGDPG
LSVFFLSLED DLMRLFGGER VSKMMLAMGM GEEEELGHKW LNKSIENAQR KVEGRNFDIR
KHLLEYDDVM NQQRMAVYGE RDYILYSDDI SPRVEEIISE VTEETIEDIS GNKKNVDALE
VTKWLNSYLI GIDEDAANKA VEGGVDNAVK NLTNLLLEAY RKKASEIDEK IFREVEKNIF
LSIIDNRWKD HLFAMDSLRE GIGLRGYAEK NPLTEYKLEG YKMFMATMNV IHNELVNLIM
RVRIIPNSFD TIERESAFDG GVEEKSSASA MNGGNAQAIQ SKVKNAQPNV KMAQKIGRND
PCPCGSGKKY KHCHGKDNPQ
