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Database: UniProt
Entry: C5CCH8_MICLC
LinkDB: C5CCH8_MICLC
Original site: C5CCH8_MICLC 
ID   C5CCH8_MICLC            Unreviewed;       346 AA.
AC   C5CCH8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-SEP-2017, entry version 55.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   OrderedLocusNames=Mlut_12850 {ECO:0000313|EMBL:ACS30790.1};
OS   Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC
OS   3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus
OS   lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS30790.1, ECO:0000313|Proteomes:UP000000738};
RN   [1] {ECO:0000313|Proteomes:UP000000738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC   NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX   PubMed=19948807; DOI=10.1128/JB.01254-09;
RA   Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F.,
RA   Dover L.G., Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N.,
RA   Lapidus A., Lowry S.R., Lykidis A., Mahillon J., Markowitz V.,
RA   Mavromatis K., Mukamolova G.V., Oren A., Rokem J.S., Smith M.C.,
RA   Young D.I., Greenblatt C.L.;
RT   "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT   free-living actinobacterium.";
RL   J. Bacteriol. 192:841-860(2010).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01464, ECO:0000256|SAAS:SAAS00541936}.
CC   -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01464}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR   EMBL; CP001628; ACS30790.1; -; Genomic_DNA.
DR   RefSeq; WP_010078575.1; NZ_CABC01000012.1.
DR   ProteinModelPortal; C5CCH8; -.
DR   STRING; 465515.MlutN2_010100000707; -.
DR   EnsemblBacteria; ACS30790; ACS30790; Mlut_12850.
DR   GeneID; 7985864; -.
DR   KEGG; mlu:Mlut_12850; -.
DR   PATRIC; fig|465515.4.peg.1226; -.
DR   eggNOG; ENOG4107RTU; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   HOGENOM; HOG000245915; -.
DR   KO; K03074; -.
DR   OMA; VNQTLMR; -.
DR   OrthoDB; POG091H02G4; -.
DR   Proteomes; UP000000738; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01464_B; SecF_B; 1.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR005665; SecF_bac.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018194};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000738};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018303};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018248};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000738};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018306};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018265};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00018174};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425232}.
FT   TRANSMEM     27     48       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    143    162       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    169    187       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    193    210       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    254    273       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    279    305       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   346 AA;  36828 MW;  ED738C0E1A858855 CRC64;
     MNRFADWGNA LYSGRISYPF IQRWRRWFAL AALLLVLAGG LTALRGGFNL GIEFRGGSEF
     TVSQTASTDV AAGERAVTDV LADGHATVTN VAPGTVRVQT EQLDDAQTRA VAANLQEAYG
     VGPDQVTSTF VGPTWGAAVS QQALIGLVIF VVLVALFMAV YFRTWKMSLA AVLGMLYVVA
     LTAGIYGATG FEITPSAIIG FLTILSYALY DTVVVFDKIR ENTIGAGEDP ERSFVENVNL
     AVNQTLVRSI TTSVVGILPV GSILFIGAGL LGAGTLRDIA LALFVGIIVG TLSTLFLQAP
     LYALLRRNDP DVRDHDARAA ARAARERASE AVTDPDVAPW DDGARL
//
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