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Database: UniProt
Entry: A0A495PXW4_9FLAO
LinkDB: A0A495PXW4_9FLAO
Original site: A0A495PXW4_9FLAO 
ID   A0A495PXW4_9FLAO        Unreviewed;      1201 AA.
AC   A0A495PXW4;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=ABC-2 family transporter {ECO:0000313|EMBL:RKS55281.1};
GN   ORFNames=BC962_0240 {ECO:0000313|EMBL:RKS55281.1};
OS   Gillisia mitskevichiae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Gillisia.
OX   NCBI_TaxID=270921 {ECO:0000313|EMBL:RKS55281.1, ECO:0000313|Proteomes:UP000276282};
RN   [1] {ECO:0000313|EMBL:RKS55281.1, ECO:0000313|Proteomes:UP000276282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19839 {ECO:0000313|EMBL:RKS55281.1,
RC   ECO:0000313|Proteomes:UP000276282};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RKS55281.1}.
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DR   EMBL; RBLG01000001; RKS55281.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495PXW4; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000276282; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF12730; ABC2_membrane_4; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        100..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        317..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        436..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        468..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        520..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        562..584
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          878..1069
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   1201 AA;  138003 MW;  928C22EA4EE4B9F6 CRC64;
     MKEIYLFELK YRLRRPATYI YLFLMFLIPL LFAVFEKSNT AQYTNSPNAI MGVLGGMSIL
     CLFFYAAIMG VAVYRDEEHR TAQTYFTFPI TEKNYILGRF WGSFTIVTFL NIAAVLGAMF
     GFAIGIFLDR PDYGTYTSFN IASYFYPFVY LLTFNAFFIG SLFFGLMTFF KRMPILYLGG
     IVIFILTIVS SRLLANLDTE WLSIYVDPFG NKAQNFIDKY WSVHELNTTQ LSLTGKFLLN
     RMIWLGIAIA IFVFTLLRFS YKGFLSSKKK QNTKEGKEVY STNNPLPKIV QVFNSKARRE
     NLWSLSKIEF LSIVKETVFI ILMVIGIVIA GFIAYQSNQI YGTPSMPLTR YMVAQIAGGI
     SLFSVIILII YAGEAVHRTR QNKTFEFYDA LPVSNNTLYL SKIISLIGVA VLLTLISIVV
     GIIYQTVNGY FNYELGMYFI FNFARIFPTY ITTLLLAFFI HVLVNNKFLG HFIVIVIYIG
     LPLLFTLAFK TSNPLLIFGG TPGGFLSDLN GFGHYLVGEF WLNTYWVLFT CILAVIGKVF
     WNRGFFSSGK ERLRVAKQRF SGRTIAYSLV LVFAFASVGA YSYYNLKVLN KLEDGNYGEK
     VNADAEKKYG KYIGKPHIQV LDLKAFIDIF PEERRVEAKG EFKVVNNFEV AIDTVLMEVK
     FPIAATRITK VIYNNVELKP FLKDTVYRLF MYKLPKALQP KETASLVIET KAITKGFSAD
     SETAVLDNGT FFTDAIFPSF HYDRALSDNG VRIKNGLEKL DYLYPPRTDS IALKKNLFNE
     DANYMTFEAT ISTAKGQTAL APGLLTKKWE ENERSYFNYK LEEKSDYFFS FVSADYEVKK
     DSWTAPSGKK VDIEIYHSEK HNRNLEYFIK GIKISLDYNS KNFFEYPYSV IRIIEFPAHS
     NYAQSFATTI PYSEDFGFVA DFSKAEDYNY AFRVTSHEVA HQWWGHIVTP SKTSGANIIS
     ETLSEYVSLM TMKKEYGENG IKSFLKNSLD TYLSSRQFSF KPERSLMNVE IADYIWYRKG
     SMIMYDLQDV IGENKVNAGL RSFLEEFKYN EKGYYATSED LYKAIYKVAP DSLKYKVDDG
     FKEIVLYENR VIEAKTKELK SGKWETTFTV NSKKIYYDDA GKEREIDTKK NLVDIGLFGE
     DVVNDEKVTI KDPFYFELKW LEPGDNKFTI ITDKKPLKAG IDPYNKLIDR NSDDNLKSIE
     E
//
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