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Database: UniProt
Entry: A0A1H7T727_9GAMM
LinkDB: A0A1H7T727_9GAMM
Original site: A0A1H7T727_9GAMM 
ID   A0A1H7T727_9GAMM        Unreviewed;       658 AA.
AC   A0A1H7T727;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein TonB {ECO:0000256|RuleBase:RU362123};
GN   ORFNames=SAMN05216262_12324 {ECO:0000313|EMBL:SEL80680.1};
OS   Colwellia chukchiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=641665 {ECO:0000313|EMBL:SEL80680.1, ECO:0000313|Proteomes:UP000199297};
RN   [1] {ECO:0000313|Proteomes:UP000199297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9127 {ECO:0000313|Proteomes:UP000199297};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interacts with outer membrane receptor proteins that carry
CC       out high-affinity binding and energy dependent uptake into the
CC       periplasmic space of specific substrates. It could act to transduce
CC       energy from the cytoplasmic membrane to specific energy-requiring
CC       processes in the outer membrane, resulting in the release into the
CC       periplasm of ligands bound by these outer membrane proteins.
CC       {ECO:0000256|RuleBase:RU362123}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004383, ECO:0000256|RuleBase:RU362123}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004383,
CC       ECO:0000256|RuleBase:RU362123}; Periplasmic side
CC       {ECO:0000256|ARBA:ARBA00004383, ECO:0000256|RuleBase:RU362123}.
CC   -!- SIMILARITY: Belongs to the TonB family. {ECO:0000256|ARBA:ARBA00006555,
CC       ECO:0000256|RuleBase:RU362123}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362123}.
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DR   EMBL; FOBI01000023; SEL80680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7T727; -.
DR   STRING; 641665.GCA_002104455_02297; -.
DR   Proteomes; UP000199297; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031992; F:energy transducer activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0015891; P:siderophore transport; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd07341; M56_BlaR1_MecR1_like; 1.
DR   Gene3D; 3.30.1150.10; -; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR008756; Peptidase_M56.
DR   InterPro; IPR003538; TonB.
DR   InterPro; IPR006260; TonB/TolA_C.
DR   InterPro; IPR037682; TonB_C.
DR   NCBIfam; TIGR01352; tonB_Cterm; 1.
DR   PANTHER; PTHR34978; POSSIBLE SENSOR-TRANSDUCER PROTEIN BLAR; 1.
DR   PANTHER; PTHR34978:SF3; SLR0241 PROTEIN; 1.
DR   Pfam; PF05569; Peptidase_M56; 1.
DR   Pfam; PF03544; TonB_C; 1.
DR   PRINTS; PR01374; TONBPROTEIN.
DR   SUPFAM; SSF74653; TolA/TonB C-terminal domain; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW   ECO:0000256|RuleBase:RU362123};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU362123};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362123};
KW   Protein transport {ECO:0000256|RuleBase:RU362123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199297};
KW   Signal-anchor {ECO:0000256|RuleBase:RU362123};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362123};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362123};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362123}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362123"
FT   TRANSMEM        49..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362123"
FT   TRANSMEM        109..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362123"
FT   TRANSMEM        219..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362123"
FT   DOMAIN          27..303
FT                   /note="Peptidase M56"
FT                   /evidence="ECO:0000259|Pfam:PF05569"
FT   DOMAIN          579..656
FT                   /note="TonB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03544"
FT   REGION          391..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  73606 MW;  987FCEA95631720A CRC64;
     MMPESLFNSP IFAALAVTLI HFLWQGVLVA LVLKMLLSLI SYRKPQLRYA LSTLAMLANL
     LLPFITFFVV YDNEYRHATS FIHTLPLLDQ SYYFEHMATN AWYIEWLEYL PILSIIWLSI
     VSALALKLTI ELYNVNQLSA RGCVTPNLAL QARFDALVNK VALRHNVKLL ISNSTNVPMA
     IGWLKPVVLI PFSMLSGLSP QQLDMLLLHE LAHIRRHDYL VNFFQTLIEI LLFFHPCVRW
     VSKQMRNERE FCSDDIAVQH SGCSLAYAHT LTDTASLCQQ QRQSSIPSMA MAASGGDLKL
     RVVRLLDQHH CSKSTESGKW LASATILIGM IFLIAKHSPS LPVIDLQSGS ISLQSSTLEF
     NNRIGNYVPK VLEQSHNSTS LARQLLAIDG GSARTSQQPT RTADSVNQLP HNPTQDVHQA
     KTVPNNRNLT NQSVSSGYEN ELPIVQQKAN TSPSHHQSLS ASVKSAAGQS QLNDKLTTTN
     KKSISELAFE RTDSKNAAVS ANPYSQQLVS LLNEPEASSE THIAALSKTH YGNSNQLRSR
     HSPKPDFTLV NKTTKQNTSS ALPTLKSSLM AAKLLRSVEP KYPIAAKRKG IELEIMVEFT
     IDKNGLVKDI QFESKNRASY FRNTIRNAME KWRFLPAKEN GRAVPSKMSK IFSFSLLR
//
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