SECA_HAEIN
ID SECA_HAEIN Reviewed; 901 AA.
AC P43803;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=HI_0909;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2] {ECO:0007744|PDB:1OZB}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 875-901 IN COMPLEX WITH SECB AND
RP ZINC, MUTAGENESIS OF ARG-878; ASN-879; LYS-888; LYS-889 AND LYS-891, AND
RP COFACTOR.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=14517549; DOI=10.1038/nsb980;
RA Zhou J., Xu Z.;
RT "Structural determinants of SecB recognition by SecA in bacterial protein
RT translocation.";
RL Nat. Struct. Biol. 10:942-947(2003).
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 both as a receptor for the
CC preprotein-SecB complex and as an ATP-driven molecular motor driving
CC the stepwise translocation of polypeptide chains across the membrane.
CC {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 ECO:0000269|PubMed:14517549};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14517549};
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Part of the essential
CC Sec protein translocation apparatus which comprises SecA, SecYEG and
CC auxiliary proteins SecDF-YajC and YidC (By similarity). Forms a complex
CC with SecB (PubMed:14517549). {ECO:0000255|HAMAP-Rule:MF_01382,
CC ECO:0000269|PubMed:14517549}.
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; L42023; AAC22566.1; -; Genomic_DNA.
DR PIR; H64101; H64101.
DR RefSeq; NP_439069.1; NC_000907.1.
DR RefSeq; WP_005693259.1; NC_000907.1.
DR PDB; 1OZB; X-ray; 2.80 A; I/J=875-901.
DR PDBsum; 1OZB; -.
DR AlphaFoldDB; P43803; -.
DR SMR; P43803; -.
DR IntAct; P43803; 1.
DR STRING; 71421.HI_0909; -.
DR PRIDE; P43803; -.
DR EnsemblBacteria; AAC22566; AAC22566; HI_0909.
DR KEGG; hin:HI_0909; -.
DR PATRIC; fig|71421.8.peg.950; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_6; -.
DR OMA; MVHYDVQ; -.
DR PhylomeDB; P43803; -.
DR BioCyc; HINF71421:G1GJ1-948-MON; -.
DR EvolutionaryTrace; P43803; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015462; F:ABC-type protein transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0043952; P:protein transport by the Sec complex; IBA:GO_Central.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm;
KW Membrane; Metal-binding; Nucleotide-binding; Protein transport;
KW Reference proteome; Translocase; Translocation; Transport; Zinc.
FT CHAIN 1..901
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000109586"
FT REGION 848..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:14517549, ECO:0007744|PDB:1OZB"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:14517549, ECO:0007744|PDB:1OZB"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:14517549, ECO:0007744|PDB:1OZB"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382,
FT ECO:0000269|PubMed:14517549, ECO:0007744|PDB:1OZB"
FT MUTAGEN 878
FT /note="R->A: Binds zinc, unable to bind secB."
FT /evidence="ECO:0000269|PubMed:14517549"
FT MUTAGEN 879
FT /note="N->A: Binds zinc, unable to bind secB."
FT /evidence="ECO:0000269|PubMed:14517549"
FT MUTAGEN 888
FT /note="K->A: Binds zinc, still binds secB."
FT /evidence="ECO:0000269|PubMed:14517549"
FT MUTAGEN 889
FT /note="K->A: Binds zinc, unable to bind secB."
FT /evidence="ECO:0000269|PubMed:14517549"
FT MUTAGEN 891
FT /note="K->A: Binds zinc, unable to bind secB."
FT /evidence="ECO:0000269|PubMed:14517549"
FT STRAND 887..889
FT /evidence="ECO:0007829|PDB:1OZB"
FT HELIX 890..892
FT /evidence="ECO:0007829|PDB:1OZB"
FT TURN 893..895
FT /evidence="ECO:0007829|PDB:1OZB"
SQ SEQUENCE 901 AA; 102587 MW; 2BD0190266BD77AE CRC64;
MSILTRIFGS RNERVLRKLK KQVVKINKME PAFEALSDDE LKAKTQEFRD RLSGGETLQQ
ILPEAFATVR EASKRVLGMR HFDVQLIGGM VLTNRCIAEM RTGEGKTLTA TLPCYLIALE
GKGVHVVTVN DYLARRDAET NRPLFEFLGM SVGVNIPGLS PEEKRAAYAA DITYATNSEL
GFDYLRDNLA HSKEERFQRT LGYALVDEVD SILIDEARTP LIISGQAENS SELYIAVNKL
IPSLIKQEKE DTEEYQGEGD FTLDLKSKQA HLTERGQEKV EDWLIAQGLM PEGDSLYSPS
RIVLLHHVMA ALRAHTLFEK DVDYIVKDGE IVIVDEHTGR TMAGRRWSDG LHQAIEAKEG
VDVKSENQTV ASISYQNYFR LYERLAGMTG TADTEAFEFQ QIYGLETVVI PTNRPMIRDD
RTDVMFENEQ YKFNAIIEDI KDCVERQQPV LVGTISVEKS EELSKALDKA GIKHNVLNAK
FHQQEAEIVA EAGFPSAVTI ATNMAGRGTD IILGGNWKAQ AAKLENPTQE QIEALKAEWE
KNHEIVMKAG GLHIIGTERH ESRRIDNQLR GRSGRQGDPG SSRFYLSLED GLMRIYLNEG
KLNLMRKAFT VAGEAMESKM LAKVIASAQA KVEAFHFDGR KNLLEYDDVA NDQRHAIYEQ
RNHLLDNDDI SETINAIRHD VFNGVIDQYI PPQSLEEQWD IKGLEERLSQ EFGMELPISN
WLEEDNNLHE ESLRERIVEI AEKEYKEKEA LVGEDAMRHF EKGVMLQTLD ELWKEHLASM
DYLRQGIHLR GYAQKDPKQE YKKESFRMFT EMLDSLKHQV ITALTRVRVR TQEEMEEAER
ARQEMAARIN QNNLPVDENS QTTQNSETED YSDRRIGRNE PCPCGSGKKY KHCHGSRVAR
Q
