ID   C5J6Z8_MYCCR            Unreviewed;       995 AA.
AC   C5J6Z8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   01-MAY-2013, entry version 31.
DE   RecName: Full=Protein translocase subunit SecA;
GN   Name=secA; OrderedLocusNames=MCJ_005620;
OS   Mycoplasma conjunctivae (strain ATCC 25834 / HRC/581 / NCTC 10147).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=572263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25834 / HRC/581 / NCTC 10147;
RX   PubMed=19534756; DOI=10.1186/1471-2105-10-S6-S7;
RA   Calderon-Copete S.P., Wigger G., Wunderlin C., Schmidheini T.,
RA   Frey J., Quail M.A., Falquet L.;
RT   "The Mycoplasma conjunctivae genome sequencing, annotation and
RT   analysis.";
RL   BMC Bioinformatics 10:S7-S7(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 as an ATP-driven molecular
CC       motor driving the stepwise translocation of polypeptide chains
CC       across the membrane (By similarity).
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 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm. Note=Distribution is 50-50 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SecA family.
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DR   EMBL; FM864216; CAT05261.1; -; Genomic_DNA.
DR   RefSeq; YP_002961064.1; NC_012806.1.
DR   STRING; 45361.MCJ_005620; -.
DR   EnsemblBacteria; CAT05261; CAT05261; MCJ_005620.
DR   GeneID; 7989356; -.
DR   KEGG; mco:MCJ_005620; -.
DR   PATRIC; 20007327; VBIMycCon56923_0539.
DR   HOGENOM; HOG000218169; -.
DR   KO; K03070; -.
DR   ProtClustDB; PRK12903; -.
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:HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:HAMAP.
DR   GO; GO:0017038; P:protein import; IEA:InterPro.
DR   GO; GO:0006605; P:protein targeting; IEA:HAMAP.
DR   Gene3D; 1.10.3060.10; -; 1.
DR   Gene3D; 3.90.1440.10; -; 1.
DR   HAMAP; MF_01382; SecA; 1; -.
DR   InterPro; IPR001650; Helicase_C.
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; PF00271; Helicase_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; SSF81767; SecA_PP_bd; 1.
DR   SUPFAM; SSF81886; SecA_SW; 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; Complete proteome; Cytoplasm; Membrane;
KW   Nucleotide-binding; Protein transport; Translocation; Transport.
FT   NP_BIND      98    105       ATP (By similarity).
SQ   SEQUENCE   995 AA;  114425 MW;  A57B32E61B3DF7E2 CRC64;
     MKSATNFFTM SSEMRLAYRL LKQINNKRAY YAAMSDDQLA NQTYELKLRL SRGEKHEDIR
     VDAFAVAREA TKRVLNKYPY DVQILGGLIL DMGSVAEMKT GEGKTIAAIA PVYLNALKGE
     GVIVSTVNEY LAERDAADNG KVFNFLGLSV GVNRAGMDSR TKKIMYSADI TYSIHSELGF
     DYLRDNMVFN KEEKVQRSLN FCLLDEIDSI LIDEAKTPLI ISGGQQLNPG DYYSANQFVQ
     TLVDDDFYVD EETKGIKLND QGIDKANAFF KTKNLYEIGN SELVHRIQNA LRANKVMKKD
     VEYIVLDDKI ELVDQFTGRI MQGRSYSEGL QQALQAKENL EIEPETKTLA TITYQNFFRL
     FKKLSGMTGT AKTEEQEFID VYNMRVNVIP TNKPIARLDD SDLIFGTLHA KNQAIIAEVE
     RVHKKGQPIL IGTSQVADSE TLSDMLRERG LSHTVLNAKQ NEYEAEIISK AGVKNAITIA
     TNMAGRGTDI KLDSEVIDLG GLYILGTDKA ESRRIDNQLR GRSGRQGDIG YSRFYISIED
     PLLRRFSNFE QIQQVYGSDK SLEPIKGKFI KKTLINAQKK IEGFNFDMRK SVLSYDDVIR
     QQRDLIYTQR NILLESDNFD HYIKRMIIRT VDIILGFDFI SLPNQEIHYT NLVNYLNDNL
     SRITHYDFSE LKLYNYPYDE VAKVIIEQLE TIYFEQLQPQ LKENLGETYY ENERYIILSS
     LDHYWQSHID TIDKLRSSAN LVQYSQKNPY QIFIEESTKK FNILISESAN QAIVSLFNNE
     NARKIVYNEY TLSNGQILSF AEDTPIELIE QIIKNNEERI EHEKQLAIYN SDEFIYKQLE
     DLNIKLVQDD LESDFQIFAL SSGKQIQIKR SFSLTDKRTI LVSMNEDELK NQLENDNQNS
     SLDSQQLSSE LSQPEDLSNQ NSFTEKSVYE IEQENLANFA NPNFSEVNEN NLQAPVEQNF
     DDEIETFFNQ NEKEKQQNSY KNIDNLSDLD NRDIF
//