ID A0A660HNL2_ZIZJU Unreviewed; 837 AA.
AC A0A660HNL2;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
DE EC=7.4.2.8 {ECO:0000256|HAMAP-Rule:MF_01382};
GN Name=secA {ECO:0000256|HAMAP-Rule:MF_01382,
GN ECO:0000313|EMBL:AYJ01562.1};
GN ORFNames=CWO85_01865 {ECO:0000313|EMBL:AYJ01562.1};
OS Ziziphus jujuba witches'-broom phytoplasma.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrV (Elm yellows group).
OX NCBI_TaxID=135727 {ECO:0000313|EMBL:AYJ01562.1, ECO:0000313|Proteomes:UP000272462};
RN [1] {ECO:0000313|EMBL:AYJ01562.1, ECO:0000313|Proteomes:UP000272462}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jwb-nky {ECO:0000313|EMBL:AYJ01562.1};
RX PubMed=30231900; DOI=.1186/s12864-018-5075-1;
RA Wang J., Song L., Jiao Q., Yang S., Gao R., Lu X., Zhou G.;
RT "Comparative genome analysis of jujube witches'-broom Phytoplasma, an
RT obligate pathogen that causes jujube witches'-broom disease.";
RL BMC Genomics 19:689-689(2018).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000256|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000256|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000256|ARBA:ARBA00007650,
CC ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
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DR EMBL; CP025121; AYJ01562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A660HNL2; -.
DR KEGG; pzi:CWO85_01865; -.
DR OrthoDB; 9805579at2; -.
DR Proteomes; UP000272462; 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: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; cd17928; DEXDc_SecA; 1.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 1.10.3060.10; Helical scaffold and wing domains of SecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 3.90.1440.10; SecA, preprotein cross-linking domain; 1.
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 NCBIfam; TIGR00963; secA; 1.
DR PANTHER; PTHR30612:SF0; CHLOROPLAST PROTEIN-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR30612; SECA INNER MEMBRANE COMPONENT OF SEC PROTEIN SECRETION SYSTEM; 1.
DR Pfam; PF21090; P-loop_SecA; 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; SSF81886; Helical scaffold and wing domains of SecA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF81767; Pre-protein crosslinking domain of SecA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01382};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01382};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01382}; Reference proteome {ECO:0000313|Proteomes:UP000272462};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01382};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01382}.
FT DOMAIN 1..571
FT /note="SecA family profile"
FT /evidence="ECO:0000259|PROSITE:PS51196"
FT DOMAIN 87..246
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 411..581
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT BINDING 493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
SQ SEQUENCE 837 AA; 96980 MW; 0222AC26B32EE53F CRC64;
MFNFVKKFFN SSNKYLKKAQ LLVNKMSNFS EGFAKLNDDD FPKETERLKK MYQAGTSLND
LLPEAFALTK EACTRVTGLT PYNVQLLGAV ILYQGQIAEM KTGEGKTLTS VMPAYLNALS
GEGVHIVTVN EYLACRESEG EIGDVFRFLG LTVGLNIKDK NIEEKKLAYK CDILYSTNSE
LGFDYLRDNI QNEIENLLMT REYNYAIIDE VDSILIDEAR TPLIISSPAK QGIKFYRDAN
RFAKTLKENG YIIDLESKTI ELSEEGIAKA ETFFQIKNLY SGNNYSLLHC IKNALKAVFI
MNKNKDYLVD NNKVLIIDQF TGRVLQGRQF SDGLHQALEA KEGCSIEGET EINATITYQN
FFRIYKKISG MTGTAKTEEK EFISIYNMRV IEIPTNKLMI RKDMPDFVFA TLDQKWESLI
QDIEERYKNK QPVLIGTVTV EVSEQISINL KKRKIPHEIL NAKNHLKEAE IIAKAGQKGS
ITIATNMAGR GTDIRLGEGV VELGGLAVLG TERHESRRID NQLRGRAGRQ GDPGYSRFFV
SAEDELVQRF GGQRIQKMIM LLNKTQDNQG QNKPISYKFF TKFFTNIQKK IESSNFDYRK
FILQFDSVLD VQRKIIYTQR REILMLDNIE DLVINIIHKT VNKKIKYFLS NKIGKIEYQN
LLDFIDYLEK LFLPQGILKL EELQQIKENK NNFEKEIIEL VHEKIKNILE QHKQNLIIDG
QDYYFQTLRF IMLQNIDNHF KRHMSDMNML SKSINFLSYG QQNVLTVYQD TGCTFFNEMM
ENICFETTRI ILKFFCSKED FLERKQQEQI LSKNNLKKDI INRKNRRKHK SVKTPWN
//
