ID T2KJX5_FORAG Unreviewed; 447 AA.
AC T2KJX5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN ORFNames=BN863_5820 {ECO:0000313|EMBL:CDF78294.1};
OS Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 /
OS M-2Alg 35-1).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1347342 {ECO:0000313|EMBL:CDF78294.1, ECO:0000313|Proteomes:UP000016160};
RN [1] {ECO:0000313|EMBL:CDF78294.1, ECO:0000313|Proteomes:UP000016160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901
RC {ECO:0000313|Proteomes:UP000016160};
RX PubMed=23995932; DOI=10.1128/AEM.01937-13;
RA Mann A.J., Hahnke R.L., Huang S., Werner J., Xing P., Barbeyron T.,
RA Huettel B., Stueber K., Reinhardt R., Harder J., Gloeckner F.O.,
RA Amann R.I., Teeling H.;
RT "The genome of the alga-associated marine flavobacterium Formosa agariphila
RT KMM 3901T reveals a broad potential for degradation of algal
RT polysaccharides.";
RL Appl. Environ. Microbiol. 79:6813-6822(2013).
CC -!- FUNCTION: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
CC {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC proteins may be involved. Interacts with SecA. {ECO:0000256|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01465}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003484}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003484}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC {ECO:0000256|ARBA:ARBA00005751, ECO:0000256|HAMAP-Rule:MF_01465,
CC ECO:0000256|RuleBase:RU004349}.
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DR EMBL; HG315671; CDF78294.1; -; Genomic_DNA.
DR RefSeq; WP_038527334.1; NZ_HG315671.1.
DR AlphaFoldDB; T2KJX5; -.
DR STRING; 1347342.BN863_5820; -.
DR PATRIC; fig|1347342.6.peg.586; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_10; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000016160; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.3370.10; SecY subunit domain; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR NCBIfam; TIGR00967; 3a0501s007; 1.
DR PANTHER; PTHR10906:SF9; PREPROTEIN TRANSLOCASE SUBUNIT SCY1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01465};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01465}; Reference proteome {ECO:0000313|Proteomes:UP000016160};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01465};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01465}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 74..99
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 214..238
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 447 AA; 48824 MW; C0824D3478B71C5B CRC64;
MKFIETLKNV WKIEELRNRI ILTVGLLLVY RFGAQVVLPG IDAAQLETLQ SNTDSGLLGL
LNAFTGGAFA NASIFALGIM PYISASIVVQ LMGIAIPYLQ KLQKEGASGQ KKINQITRWL
TIAICLVQAP GYLASLPSLG IPQSAFLLGQ GGLFYFSSII ILVTGCIFAM WLGEKITDKG
IGNGISLLIM VGIIARMPLS FFQNAASRLE GNNVMLILIE LVLWFAIIFA SIMLIMAVRK
IAVQYARRTA TGGYEKNIMG SRQYIPLKLN ASGVMPIIFA QAIMFVPGLI GGTSMMKDSA
AGQWLQSQFS DIFGFWYNLL FAFLIIIFTY FYTAITVPTN KMADDLKRSG GFIPGIRPGS
ETSEYLDKIM SQITLPGSIF LALIAVFPAI VVKLMNVQSG WALFFGGTSL LILVGVAIDT
MQQVNSYLLN RHYDGLMKTG KNRKAVA
//
