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Database: UniProt
Entry: K0CAT8_ALCDB
LinkDB: K0CAT8_ALCDB
Original site: K0CAT8_ALCDB 
ID   K0CAT8_ALCDB            Unreviewed;      1089 AA.
AC   K0CAT8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Transporter, MscS family {ECO:0000313|EMBL:AFT69728.1};
GN   OrderedLocusNames=B5T_01446 {ECO:0000313|EMBL:AFT69728.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS   B-5) (Alloalcanivorax dieselolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alloalcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT69728.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT69728.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC       {ECO:0000256|ARBA:ARBA00008017}.
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DR   EMBL; CP003466; AFT69728.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0CAT8; -.
DR   STRING; 930169.B5T_01446; -.
DR   KEGG; adi:B5T_01446; -.
DR   PATRIC; fig|930169.3.peg.1421; -.
DR   eggNOG; COG1196; Bacteria.
DR   eggNOG; COG3264; Bacteria.
DR   HOGENOM; CLU_007829_3_0_6; -.
DR   Proteomes; UP000006286; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 1.10.287.1260; -; 1.
DR   Gene3D; 2.30.30.60; -; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR049142; MS_channel_1st.
DR   InterPro; IPR049278; MS_channel_C.
DR   InterPro; IPR023408; MscS_beta-dom_sf.
DR   InterPro; IPR006685; MscS_channel_2nd.
DR   InterPro; IPR011066; MscS_channel_C_sf.
DR   InterPro; IPR006686; MscS_channel_CS.
DR   InterPro; IPR011014; MscS_channel_TM-2.
DR   InterPro; IPR025692; MscS_IM_dom1.
DR   InterPro; IPR024393; MscS_porin.
DR   PANTHER; PTHR30347:SF8; MECHANOSENSITIVE CHANNEL MSCK; 1.
DR   PANTHER; PTHR30347; POTASSIUM CHANNEL RELATED; 1.
DR   Pfam; PF21088; MS_channel_1st; 1.
DR   Pfam; PF00924; MS_channel_2nd; 1.
DR   Pfam; PF21082; MS_channel_3rd; 1.
DR   Pfam; PF12795; MscS_porin; 1.
DR   Pfam; PF12794; MscS_TM; 1.
DR   SUPFAM; SSF82689; Mechanosensitive channel protein MscS (YggB), C-terminal domain; 1.
DR   SUPFAM; SSF82861; Mechanosensitive channel protein MscS (YggB), transmembrane region; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS01246; UPF0003; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        474..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        595..614
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        626..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        661..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        695..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        760..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        813..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        855..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        882..909
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..257
FT                   /note="Mechanosensitive ion channel MscS porin"
FT                   /evidence="ECO:0000259|Pfam:PF12795"
FT   DOMAIN          475..793
FT                   /note="Mechanosensitive ion channel inner membrane"
FT                   /evidence="ECO:0000259|Pfam:PF12794"
FT   DOMAIN          854..895
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          897..962
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          972..1053
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1069..1089
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          67..125
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          256..283
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1089 AA;  121784 MW;  740CD92EAE66DCB0 CRC64;
     MAAAQGSGFS LPGIGDLEKQ LTGGGDSADT QKEGKPAPER DLLEETLKLR KEIDANHEQI
     KKLGEQQKAL PREKAALQDE LEKIRRESTI DWAERYQSLS ISALAEELGQ QLQALERNQE
     KLADAASDVT SSQTLPERAQ NTISDSLAEA DDIRRRLNRP SVAETLSEAE VQNLQVKLAV
     LDSRIELRNQ ELAVASSSEQ RSRLRQRVLE ADAELIQKQL DVLQPLINRR RQQQLQDELQ
     AASVDLPAGV ADHPELAAAQ ERNKTLRKQL VQTSEEVNDL LRENVATKTQ LDRVRALSAT
     VNDQIRMLDG SLLLSRILYE QQKNLPDFKP REGLPKAIGD TRLRQFEIGQ QRQQTEADIL
     RIDDQGISPE DRAALQDALG SLHDIHVELL NQLDTELGRK LNLLVRLNLV QDQLVDVSRN
     LHDTISEQTF WMPSTQPINL SWLREFPAQV RDQMTYIPWA ETGKRSLRLL QDKWPWLILP
     AVLAAALLVW RKRLRTRIRK LNSDIGFLRR DSQLHTPLAI LMTTLMCLPG PLVLSLLAWG
     LWIQPGTLST VLGAALFKVA LLWLVFEMCY RLLARDGIAQ RHFRWSADGN TQLRRRLLAV
     GLAMVPMTLI IAFGEQWPAQ LNNDRIGLVI MVFGLAVMGI MLTRVALHFP ITRFSTAYKT
     VAALVCGGLP FALIVVIGLG YYYTTVRLSG RIIDSFYLLL LWTLIDATAV RGLAVAAQRL
     AYKRALAQRD SDTKDTSVEG IEVEEPQLDL ERVNQQSLRL IRMALVVVFG LLFYWVWADI
     LSAFSYTENI LLWETTEGSG STLTQVPISL GDVMFALAAG VVTLMLALNL PGLLEVLLLS
     RMNLKQGSSY ATTTLLSYLI TAVGVMVVLG SLGLTWNKLQ WLVAALGVGL GFGLQQIFAN
     FVSGIIILFE RPIRIGDVIT IGTLSGTVSR VRVRATTVID FDRKEIIIPN QTFVTEQLIN
     WSLSDTVTRL IITVGFAYGS DLNSCREILQ TVARDHPKVM KDPEPMILFM GFGASTLDHE
     LRVYVKEIGD RLSTTDELNR RIDQLCRDRG VEIAFSQMDI HIRSINGGEN LTIPGERRES
     GNGDPKTGA
//
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