ID   SECA_LARHH              Reviewed;         906 AA.
AC   C1D5K2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   11-NOV-2015, entry version 48.
DE   RecName: Full=Protein translocase subunit SecA {ECO:0000255|HAMAP-Rule:MF_01382};
GN   Name=secA {ECO:0000255|HAMAP-Rule:MF_01382};
GN   OrderedLocusNames=LHK_03041;
OS   Laribacter hongkongensis (strain HLHK9).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Laribacter.
OX   NCBI_TaxID=557598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLHK9;
RX   PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA   Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O.,
RA   Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J.,
RA   Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S.,
RA   Yuen K.-Y.;
RT   "The complete genome and proteome of Laribacter hongkongensis reveal
RT   potential mechanisms for adaptations to different temperatures and
RT   habitats.";
RL   PLoS Genet. 5:E1000416-E1000416(2009).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. Has a central role
CC       in coupling the hydrolysis of ATP to the transfer of proteins into
CC       and across the cell membrane, serving both as a receptor for the
CC       preprotein-SecB complex and as an ATP-driven molecular motor
CC       driving the stepwise translocation of polypeptide chains across
CC       the membrane. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01382};
CC       Note=May bind 1 zinc ion per subunit. {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-YajC and YidC. {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-
CC       Rule:MF_01382}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01382}.
CC       Note=Distribution is 50-50. {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; CP001154; ACO76019.1; -; Genomic_DNA.
DR   RefSeq; WP_012698482.1; NC_012559.1.
DR   STRING; 557598.LHK_03041; -.
DR   EnsemblBacteria; ACO76019; ACO76019; LHK_03041.
DR   KEGG; lhk:LHK_03041; -.
DR   PATRIC; 22302842; VBILarHon49832_2775.
DR   eggNOG; ENOG4105CI6; Bacteria.
DR   eggNOG; COG0653; LUCA.
DR   HOGENOM; HOG000218168; -.
DR   KO; K03070; -.
DR   OMA; IATERHE; -.
DR   OrthoDB; EOG654P48; -.
DR   BioCyc; LHON557598:GHO5-3101-MONOMER; -.
DR   Proteomes; UP000002010; 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-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.3060.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   Gene3D; 3.90.1440.10; -; 1.
DR   HAMAP; MF_01382; SecA; 1.
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; IPR011116; SecA_Wing/Scaffold.
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; 3.
DR   SUPFAM; SSF81767; SSF81767; 1.
DR   SUPFAM; SSF81886; SSF81886; 2.
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 inner membrane; Cell membrane; Complete proteome;
KW   Cytoplasm; Membrane; Metal-binding; Nucleotide-binding;
KW   Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT   CHAIN         1    906       Protein translocase subunit SecA.
FT                                /FTId=PRO_1000184234.
FT   NP_BIND     102    109       ATP. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       890    890       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       892    892       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       901    901       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
FT   METAL       902    902       Zinc. {ECO:0000255|HAMAP-Rule:MF_01382}.
SQ   SEQUENCE   906 AA;  101119 MW;  E9BBD672BC1FC6DC CRC64;
     MIANILKKVF GSRNDRLLKQ YRAVVNRINA LESGLQTLDD AALAGKTAEF RARVEKGERL
     DSLLPEAFAV CREASRRVMG MRHFDVQLIG GMVLHDGKIA EMRTGEGKTL VATLPAYLNA
     LAGKGVHVVT VNDYLASRDA GIMAPLYNFL GLSVGVNLSQ MPHDAKQDAY AADITYGTNN
     EFGFDYLRDN MVYSPAERVQ KPLSFAIVDE VDSILIDEAR TPLIISGPAD DNVDMYRRMN
     AIPALLVRQQ AEDGEGDYWV DEKAHTVMLS EAGFEHAEAA LVAADLLKEG ESLYSAANIT
     LMHHLMAALR AHALFHRDQH YVVQDGEIVI VDEFTGRLMA GRRWSEGLHQ AVEAKEGVNI
     NRENQTLASI TFQNYFRLYK KLAGMTGTAD TEAYEFQQIY GLETVVIPTN RPMVRKDSLD
     LVYRTGQEKY NAILADITDC HQRGQPVLVG TTSIENSELL AGLLKQAGLP HNVLNAKEHA
     READIIVQAG RPGVVTVATN MAGRGTDIVL GGNIAPEIKA IESDESLTAD DRAQRIAALK
     AEWQARHDAV LAAGGLHIIG TERHESRRID NQLRGRSGRQ GDPGSSRFYL SLEDPLLRIF
     ASERVSAIMQ RLNMPEGEAI EHSWVTRAIE NAQRKVEGRN FDIRKQLLEY DDVANDQRRV
     IYQQRNEILE SEEVSDMIAA MRDDVLSQLF DTWMPPQSIE EQWDAAGLMR VLEADYQISV
     PLADWIKAEP NAELDTFKIR ILEQARALYD EKVAAVGAAS MQQFERAVLL QHFDGAWREH
     LAALDHLRQG IHLRGYAQKN PKQEYKREAF ELFSLMLDRI KREVTQIVAT VQIRSPEEAA
     AAEAFEHEER PMTYRHDEFT VEGDEAGEGN PFTAEKLAAA GVRVGRNDPC PCGSGKRYKQ
     CHGRLA
//