ID A0A495KM73_9FLAO Unreviewed; 1449 AA.
AC A0A495KM73;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Cobalt-zinc-cadmium resistance protein CzcA {ECO:0000313|EMBL:RKS02182.1};
GN ORFNames=C8C84_1885 {ECO:0000313|EMBL:RKS02182.1};
OS Flavobacterium sp. 102.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2135623 {ECO:0000313|EMBL:RKS02182.1, ECO:0000313|Proteomes:UP000270484};
RN [1] {ECO:0000313|EMBL:RKS02182.1, ECO:0000313|Proteomes:UP000270484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=102 {ECO:0000313|EMBL:RKS02182.1,
RC ECO:0000313|Proteomes:UP000270484};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000256|ARBA:ARBA00007613}.
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:RKS02182.1}.
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DR EMBL; RBKX01000001; RKS02182.1; -; Genomic_DNA.
DR OrthoDB; 9758757at2; -.
DR Proteomes; UP000270484; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.30.70.1430; Multidrug efflux transporter AcrB pore domain; 2.
DR Gene3D; 3.30.70.1440; Multidrug efflux transporter AcrB pore domain; 1.
DR Gene3D; 3.30.70.1320; Multidrug efflux transporter AcrB pore domain like; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR Gene3D; 1.20.1600.10; Outer membrane efflux proteins (OEP); 1.
DR InterPro; IPR027463; AcrB_DN_DC_subdom.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR004763; CusA-like.
DR InterPro; IPR003423; OMP_efflux.
DR NCBIfam; TIGR00914; 2A0601; 1.
DR PANTHER; PTHR32063; -; 1.
DR PANTHER; PTHR32063:SF24; CATION EFFLUX SYSTEM (ACRB_ACRD_ACRF FAMILY); 1.
DR Pfam; PF00873; ACR_tran; 1.
DR Pfam; PF02321; OEP; 2.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR SUPFAM; SSF56954; Outer membrane efflux proteins (OEP); 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 484..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 904..923
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 929..954
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 975..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1008..1030
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1042..1060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT COILED 1209..1236
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1449 AA; 160741 MW; 56A06F64951CC1C2 CRC64;
MLNKIIAFSV RNKLVIGLFT IALLLYGIYE TTKLPIDAVP DITNNQVQVI TIAPSFGATD
IERLVTFPVE QANSNISGLK EIRSFSRFGL SLVTIVFDDE TDIYWARQQV AERLQQVQTQ
IPAGIGTPEL GPVSTGLGEI YQYMVRPEKG YEEQYDETEL RTIQDWIVRR QLLGVKGVAE
VSSFGGKLKQ FEVAIESNKL HAYGLTVDDI FAALEKNNQN TGGAYIEKGA TTLFIRSEGL
IGNVEDIENI AVKATPSGIP LFLRDIAKIN IGYATRYGAM CYNDEGEVAG AIVMMLKGAN
SSEVIKNVKE RIEQIKKTLP EGVTIEPFLD RTKMVNNAIG TVEKNLMEGA LIVIFVLVLF
LGNLRAGLIV ASVIPLAMLF AIILMNTFGV SGNLMSLGAL DFGLIVDGAV IIVEAVMHQL
SHSKKFSNVA RLTQNKMDKE VENSAGKMMN SAVFGQIIIL IVYLPIFTLE GIEGKMFKPM
AQTVAFALLG AFLLSLTYIP MMSALFLSKK INHQPNFSDR MMFKLERKYQ HWLQVALNFQ
KVIIGTVIAL FVIALFLLSS LGGEFIPALE EGDFAVDTRV LTGSNLNTTI ESTQKAAHIL
KTRFPEVEKV VTKIGSGEVP TDPMPMEASD MMVILKDKSE WTSAETFDEL AEKMGKALED
VPGITAGFQY PVQMRFNELM TGARQDVVCK IFGENLDTLA LYAEKLGKIV NTVDGAEDLF
VEPVTGMPQV IIDYNRTVIA QYHLNIADIN RIVNTAFAGQ STGLVFEGEK RFELVVRLDS
EKRKNLEDVR NLLIPTPQGT QIPLSQLANV SIKNGPNQIQ REDAKRRIVV GFNVNGRDVE
SIVNELKGKV ENEIQLPAGY YTTYGGAFEN LNQAKDRLMI AVPISLLLIF ILLFFAFKSV
KHGLLIYSAI PLSAIGGIFF LALRGMPFSI SAGIGFIALF GVAVLNGIVL ISEFNRLKSE
GMDDLNRIVL MGTKVRLRPV LMTAFVASLG FLPMAISSGS GAEVQRPLAT VVIGGLMIAT
LLTLFVLPIL YVTFEKGFKM KIFNKTTLLL LLLSFCILPA KAQTKITLEE ALKTALENNQ
SVKIERLKSD YQQKLIRSAT NLPTTNVNSE FGQINSSYND TRFGISQSFD FPMVYNRQKK
VLTSEWKTAS ALVLLKEAAL KKEITQTFYA ILSLTEKEKL LQKSDTLLTE FLRKSALRLQ
KGESNILEKT TAETQLGQLK MQLLQLQQDK ELLQSIFQLL LNSENKVTPK ASSFKIERLN
GLSESTIDQH PMLQTLEQQK ETAVAQTQLE KARKFPILTL GYNNMSITGN GADNVLYDNS
TRFHSAQIGL GIPLLGGSQN AKVRAAKVQE QIVEEEYLRE KNSLKLQLQN TLLQLEKNIE
KLDYFEKIGL PNALLITETA NRQFLGGDIN YLDWVLLVNQ ALMVNNSYIE SVNAYNESII
ELNYLTSKN
//
