CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010156
UniProt Accession
Genbank Protein ID
 U00089 
Genbank Nucleotide ID
Protein Name
 Protein translocase subunit SecA 
Protein Synonyms/Alias
  
Gene Name
 secA 
Gene Synonyms/Alias
 MPN_210; MP621 
Created Date
 July 27, 2013 
Organism
 Mycoplasma pneumoniae (strain ATCC 29342 / M129) 
NCBI Taxa ID
 272634 
Lysine Modification
Position
Peptide
Type
References
31ANEVEGHKNYYRNLTacetylation[1]
268ALTELGIKHAEKNFKacetylation[1]
272LGIKHAEKNFKTDNLacetylation[1]
305VKVFEQGKEYIVRDGacetylation[1]
Reference
 [1] Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
 van Noort V, Seebacher J, Bader S, Mohammed S, Vonkova I, Betts MJ, Kühner S, Kumar R, Maier T, O'Flaherty M, Rybin V, Schmeisky A, Yus E, Stülke J, Serrano L, Russell RB, Heck AJ, Bork P, Gavin AC.
 Mol Syst Biol. 2012 Feb 28;8:571. [PMID: 22373819
Functional Description
 Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane (By similarity). 
Sequence Annotation
 NP_BIND 102 109 ATP (Potential).  
Keyword
 ATP-binding; Cell membrane; Complete proteome; Cytoplasm; Membrane; Nucleotide-binding; Protein transport; Reference proteome; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 808 AA 
Protein Sequence
MGLFNFLKLV SPRHRIYHKA SKIANEVEGH KNYYRNLTDV QLLEESNKLV DLVTKQNYTI 60
LDVAVAALAL IREVVYRETG EFAYRVQIIG AYIVLIGDFA EMMTGEGKTL TIVLAAYVSA 120
LEKRGVHVVT VNEYLAQRDA TNATKILKRV GMTVGCNFAN LAPHLKQAAF ACDVTYTTNS 180
ELGFDYLRDN MVHRFEDKKI RELHFAIVDE GDSVLIDEAR TPLIISGPAK NEFAAYVAVD 240
RFVKKLKEDE YKIDPESRAP ALTELGIKHA EKNFKTDNLF ALENSDLFHK IINALTAVKV 300
FEQGKEYIVR DGKVLIVDHF TGRILEGRSY SNGLHQAVQA KEMVEIEPEN VIVATITYQS 360
FFRLYNRLSA VSGTAFTESE EFLKIYNMVV VPVPTNRPNI RKDRADSVFG TPNIKWLAVV 420
KEVKRIHETG RPILIGTANI DDSELLHNYL QEANIPHEVL NAKNHSREAE IVAKAGQKGA 480
VTISTNMAGR GTDIRLGEGV AEMGGLYVLG TERNESRRID NQLRGRAGRQ GDRGETKFFI 540
SLGDALFKRF AHDRIERAIT KLGNDTFDSS FFSKMLSRTQ KRVEAINFDT RKNLIDYDHV 600
LASQRELIYK QRDKFLLATD LSDMIDKMLE KFVEQFCDQY RNPKNQNLVN HIALSEALNL 660
ELNMHGVISP KLFENMTFDA TVHKTHSLIG EKITNKVKVL TPPIALIRFR EIMITAMDKH 720
WIEHLDNVFK LREGVTLRSM EQTSPLNVYI RETDILFQTM LQKIARDVII QIANLATPEE 780
FDEELMKANA LKKLQALREA HEKSNEGQ 808 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0065002; P:intracellular protein transmembrane transport; IEA:HAMAP.
 GO:0017038; P:protein import; IEA:InterPro.
 GO:0006605; P:protein targeting; IEA:HAMAP. 
Interpro
 IPR027417; P-loop_NTPase.
 IPR000185; SecA.
 IPR020937; SecA_CS.
 IPR011115; SecA_DEAD.
 IPR014018; SecA_motor_DEAD.
 IPR011130; SecA_preprotein_X-link_dom.
 IPR011116; SecA_Wing/Scaffold. 
Pfam
 PF07517; SecA_DEAD
 PF01043; SecA_PP_bind
 PF07516; SecA_SW 
SMART
 SM00957; SecA_DEAD
 SM00958; SecA_PP_bind 
PROSITE
 PS01312; SECA
 PS51196; SECA_MOTOR_DEAD 
PRINTS
 PR00906; SECA.