SECA_SULMW
ID SECA_SULMW Reviewed; 1018 AA.
AC A8Z5Z5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=SMGWSS_135;
OS Sulcia muelleri (strain GWSS).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=444179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWSS;
RX PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA McCutcheon J.P., Moran N.A.;
RT "Parallel genomic evolution and metabolic interdependence in an ancient
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(2007).
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; CP000770; ABS30546.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Z5Z5; -.
DR SMR; A8Z5Z5; -.
DR STRING; 444179.SMGWSS_135; -.
DR PRIDE; A8Z5Z5; -.
DR EnsemblBacteria; ABS30546; ABS30546; SMGWSS_135.
DR KEGG; smg:SMGWSS_135; -.
DR HOGENOM; CLU_005314_3_0_10; -.
DR OMA; MVHYDVQ; -.
DR Proteomes; UP000000781; 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; 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; 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; Reference proteome; Translocase;
KW Translocation; Transport.
FT CHAIN 1..1018
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000321017"
FT BINDING 182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 200..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 699
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 1018 AA; 120328 MW; 3377CFA6052E44DE CRC64;
MIYINNIINF FFKKKNKIEI KKLKIVLNKI NFFLGKLKLY SNDELRNKTF SFKRRIKKKT
KSLYEKKFGL QKKLIYKNFI SIEEMHENKL ILSEIEEIKN NIYKEEEKIL LELLPEAFAV
VKETAKRFKE NKQIIVTSNE LDYRLSKSRS YLELKGGKTI WNNKWSYMGK ELIWNMIHYD
VQLMGGIVLH QGKIAEMYTG EGKTLVATLP IYLNALTGKG VHVVTVNEYL AKRDSEWMAP
IMEFHGLTVD CIDLYKKNSY LRRKAYEADV TYGTNNEFVF DYLRDNMVYS CKNLIQRELN
YAIIDEIDSV LIDEARTPLI ISAGVSGQVN SNYYLLKDKV KKLFKKQLYF LNKIFNLSRE
QIISGNEKEG GLNLFKVYRG LPKYKPLIKF LGEKKNRKIL EDTEYYFMQD NNKNMFIVDS
DLFFVINEKN NTVEFSEKGI NFISEEMNDP NFFILPDIHK KFIDLESLKI SKTQKEIIKN
ELITNYYNKS DKIHTVNQLI KAYTLFYKNI HYLVIDNKVK IVDEQTGRII EEKRYSDGLH
QALEAKENVN IENSSQPLAT ITLQNYFRMY KKLSGMTGTA ETEYEEFIKI YNLDVVIIPT
NKPIIRKNYE DILFRTKKEK YNAIINEIIF LSKNEKRPVL VGTTSVEISE LISRSLNIRN
INNNVLNAKH HKKEAYIIEE AGKSGIVTIA TNMAGRGTDI KISDEVKKLG GLAIIGTERH
DSRRIDRQLI GRTGRQGDPG SSKFYLSLED DLMRIFGLDR ISTILDKLGH KKGEYLTGGL
ISNSIQLAQK KIEENNFSIR KRLLEYDSVI NEQRKFIYAF RRNALNINLS SYIIYNLVDK
IDSKQRFEEF EEELFNIFKI KNLISYNTFL KKKDIKKKLY YKINKYYNIR KNKMLSKLIY
IKSYKKFCCK NKKIKSYFTY SINDRIIRLF LKEENNLYKI INNLEKKIIL YFIDDKWKTH
IHNMEDLRKY SQYSVYEQKD PIIIYKIKAF KLFNNFFYNL NKLSLTFFFN CKINNSLI
