SECA_AYWBP
ID SECA_AYWBP Reviewed; 835 AA.
AC Q2NJH2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=AYWB_304;
OS Aster yellows witches'-broom phytoplasma (strain AYWB).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; Candidatus Phytoplasma asteris.
OX NCBI_TaxID=322098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AYWB;
RX PubMed=16672622; DOI=10.1128/jb.188.10.3682-3696.2006;
RA Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A., Shevchenko D.V.,
RA Tsukerman K., Walunas T., Lapidus A., Campbell J.W., Hogenhout S.A.;
RT "Living with genome instability: the adaptation of phytoplasmas to diverse
RT environments of their insect and plant hosts.";
RL J. Bacteriol. 188:3682-3696(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 membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {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; CP000061; ABC65421.1; -; Genomic_DNA.
DR RefSeq; WP_011412585.1; NC_007716.1.
DR AlphaFoldDB; Q2NJH2; -.
DR SMR; Q2NJH2; -.
DR STRING; 322098.AYWB_304; -.
DR PRIDE; Q2NJH2; -.
DR EnsemblBacteria; ABC65421; ABC65421; AYWB_304.
DR KEGG; ayw:AYWB_304; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_0_14; -.
DR OMA; MVHYDVQ; -.
DR OrthoDB; 212453at2; -.
DR PhylomeDB; Q2NJH2; -.
DR Proteomes; UP000001934; 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 membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Translocase; Translocation; Transport.
FT CHAIN 1..835
FT /note="Protein translocase subunit SecA"
FT /id="PRO_0000320727"
FT REGION 805..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Basic and acidic 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 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 835 AA; 95749 MW; 0115AD71058AB270 CRC64;
MFNFLKKIFN SSKKALRKAR TIANKVQNLE AQIALLDDKD FATKTAELKK LFQEGKTLNQ
LLPEAYALAK EATKRVTGLT PYYVQILGAV ILHQGNIAEM KTGEGKTLTA IMPAYLNALS
GNAVHIVTVN EYLAKREFEG SIGDVFRFLG MTVGLNTKDK DQTQKQQAYL CDVLYTTNSE
LGFDYLRDNM EIEASNLVMK RPYSYAIVDE VDSILIDEAR TPLIISQSVK ETKNLYKEAQ
RFVRTLKNSH YLIELETKTI ELTEEGITKA ENFFQIDNLY NIEHASLLHH VKNALKAAFT
MHKDKDYLVD YKDGQVLIID QFTGRALPGR QFSDGLHQAL EAKEGLLIKK ETSIGATITY
QNFFRLYQKL SGMTGTAKTE EDEFRDIYNM EVIEIPTNVP MIRIDEPDFI FVSLKEKYDA
LIEELTSRHK KGQPILIGTT TVEVSEIISK KLKKHSIKHE ILNAKNHSKE AEIIAKAGLK
NAVTIATNMA GRGTDIRLGE GVKELGGLSV LGTERHESRR IDNQLRGRAG RQGDPGYSRF
FISSEDELAQ RFGGTRIEKI ISLLQKISDS ETKTSSKMVT KFFTKIQKKV ESSNFDYRKY
LLKYDDILRI QREIIYNQRK EILVSDKVEQ IVQDLMKKTL NKAIFTHFTN KPNKCQTQAL
ITFLENKFFP KQTFDLEEVQ ELCNNPKTNS LDSFQQYSFQ KVKDILQSQK DFFVKDPEKA
QYFAKGLKWI TLKIIDNYYQ RHINDMSSLR QGIGFVSYGQ QDSFIEYQKE GQVLFNNMIT
KIANDITATI LKFSFADSFQ TPPKQKVFFK NDSSDDESSK KRRTRKVRTS KKPWN
