SECA_AZOPC
ID SECA_AZOPC Reviewed; 1119 AA.
AC B6YQX8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=CFPG_337;
OS Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC Candidatus Azobacteroides.
OX NCBI_TaxID=511995;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19008447; DOI=10.1126/science.1165578;
RA Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT protist cells in termite gut.";
RL Science 322:1108-1109(2008).
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 -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; AP010656; BAG83600.1; -; Genomic_DNA.
DR RefSeq; WP_012573361.1; NC_011565.1.
DR AlphaFoldDB; B6YQX8; -.
DR SMR; B6YQX8; -.
DR STRING; 511995.CFPG_337; -.
DR EnsemblBacteria; BAG83600; BAG83600; CFPG_337.
DR KEGG; aps:CFPG_337; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR Proteomes; UP000000723; 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; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004027; SEC_C_motif.
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; PF02810; SEC-C; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
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 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 Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..1119
FT /note="Protein translocase subunit SecA"
FT /id="PRO_1000144973"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 213..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 1118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1119 AA; 129811 MW; 9A016A65060257C7 CRC64;
MNFSNILSNF FGNKSQRDLN EISPFVQKTL TIYSSVENLS NDELRGRTRE LMILLQKEIE
MEKNKIDELK ILVESLELED RETVWNEIDE IEKDIIEKQE RILDKILPEV FAIVKDTARR
FAENETIEVT ATDFDRQLAV FYDFVSIQND KAIYQNHWFA GGNEIIWNMI HYNVQLFGGI
VLHNCNPKKY IKDIEGHNFS KKIKGYIAEM ATGEGKTLAA TLPVFLNAMT HNGVHVVTIN
DYLSKRDSEW MGPLYMFHGL SVDCIDKHRP NSNERRKAYE ADITFGTNSE FGFDYLRDNM
AVNPQDLVQR KHNYAIIDEV DSVLIDDART PLIISGPVAK EDDQLYVLYR SRVENLVNVQ
KKLTNNLLIE AKKLMALEDP KQHEEGLKLL FRSYKGMPKN KALIKYLSEP GIKMSMLKTE
EFYMQQQNRE MYIITDELYF VIDEKNRSVE LTDRGIDILT GNSDDPEFFV LPDLGTKFAE
IENELITKEE KQLKKDELMQ SYAAKSERVH TINQLLKAYC LFEKDDAYVV LDNRVMIVDE
QTGRIMEGRR YSDGLHQAIE AKEHVKIEAA TQTFATITLQ NYFRMYRKLA GMTGTAETEA
GEFWDIYKLD VVVIPTNQLV IRNDKDDRLY KTAREKYAAI INEIITLREH GRPVLVGTTS
VEISELLSRM LNMRKIHHNV LNAKLHQKEA EIVAQAGQTG TVTIATNMAG RGTDIKLSTK
ARDAGGLAII GTERHDSRRI DRQLRGRSGR QGDPGSSVFF ISLEDDLMRL FASERIAKMM
DKMGFKEGEV LEAKMLNNAV ERAQKKVEEN NFGIRKRLLE YDDVMNSQRE VIYKRRHHAL
IGERIGLDII NMIYDVVNSI VEQYSNFNDY KGLKSELYKT LAIEPPISEE EFKNMKTTHL
TEVIFNTSIV NFKWKNEQIV QIVQPRIERA YKEVGNKYQN IIVPITDGRK IYNVSYHLKT
VHDTKSREII KSFEKAVLLS SIDEAWREHL REMDELHNSV QNASYENKDP LLIYKLESFN
LFKNMIDTMN KRVISILMRG QIYIKNQEVR EATPEKKTNY NHYKVRKDEL IESGRIQGRT
AKRDTRILQK IEPIRVEKTV RRNDPCPCGS GKKYKNCCF
