ID   A0A0G4KB94_9FLOR        Unreviewed;       869 AA.
AC   A0A0G4KB94;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   11-DEC-2019, entry version 16.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874};
GN   Name=secA {ECO:0000256|HAMAP-Rule:MF_01382,
GN   ECO:0000313|EMBL:CRF40066.1};
OS   Laurencia snackeyi.
OG   Plastid {ECO:0000313|EMBL:CRF40066.1}.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Ceramiales;
OC   Rhodomelaceae; Laurencieae; Laurencia.
OX   NCBI_TaxID=1858662 {ECO:0000313|EMBL:CRF40066.1};
RN   [1] {ECO:0000313|EMBL:CRF40066.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Verbruggen Heroen;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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|HAMAP-
CC       Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
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DR   EMBL; LN833431; CRF40066.1; -; Genomic_DNA.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009536; C:plastid; IEA:UniProtKB-KW.
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   HAMAP; MF_01382; SecA; 1.
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; IPR011116; SecA_Wing/Scaffold.
DR   InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR   InterPro; IPR036670; SecA_X-link_sf.
DR   PANTHER; PTHR30612; PTHR30612; 2.
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 {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01382};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874}; Plastid {ECO:0000313|EMBL:CRF40066.1};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01382,
KW   ECO:0000256|RuleBase:RU003874};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01382, ECO:0000256|RuleBase:RU003874}.
FT   DOMAIN          1..656
FT                   /note="SECA_MOTOR_DEAD"
FT                   /evidence="ECO:0000259|PROSITE:PS51196"
FT   NP_BIND         95..102
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01382"
FT   COILED          721..748
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   869 AA;  101139 MW;  1CA183140EB56323 CRC64;
     MFNFFPYNSI NKYKATIKEI NQQYCKIQQY SNSELKKQTE KLKLAIIQDN KNLDEILIEA
     FATVKEAIAR ATGIVLFDVQ ILGGIILHKG NIAEMKTGEG KTLVALLPAY LNTLNSTNVH
     IITVNDYLAK RDAKLAQTVF NYLNIQTGVI TSSTNYYNRK KEYKQDITYI TNNELGFDYL
     RDNMAINSND IIQSSLNYAI IDEVDSILID EARTPLIISG ETKISDNLYS KSKETSQKLE
     KKIHYQVDEK SRNVILTEKG VLVCEQILNI QNLYNINSPW LKYIVNALKA KELFLKNKDY
     IVKDNKVVIV DEFTGRIMEG RRWSDGLHQS IEAKENLKIE KENKTLASIT YQNLFLLYKK
     LCGMTGTAKT EENEFLNIYK MSVIEIPTNK QCIRKDLSDL VYQSEYSKWK AITNECIDMY
     QIGRPTLIGT TSIEKSELLA NMLDELDISY NLLNAKPENT NKEADIISEA GRKYKITIST
     NMAGRGTDII LGGNPHKVIQ ENLKKYIHSH INLSDYKVDQ VQHILNNTEV KVLNNFIEQA
     IQESQEIPAI VEDIINQKSC DKLYKISQKL SNEFTSICNK EKQEILALGG LYVIGTERHE
     SRRIDNQLRG RSGRQGDKGT SRFFLSLQDN LFRIFGGNKI KTLMKNLKID DNTPIESIVL
     SKSLNNAQKK VEAYFYDIRK QLFEYDEVIN NQRKAIYRER KAILNSYFTK DCIIEYGEYT
     IKEMIRLYEK EKRNIEILKQ IIQLLNIQQN ISIETIKTMK IKDLEQILFQ QFRISYDLKE
     TYLEQLRPGL IRQLEKYYLL QQIDKAWQDH IERMNLLKEY IGWRSYGQQE PLVEYKNEGF
     HLFINMTTYI RQTVIYLIMR SRLIIDLPN
//