ID A0A291R181_9BACT Unreviewed; 725 AA.
AC A0A291R181;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase C39 {ECO:0000313|EMBL:ATL49911.1};
GN ORFNames=COR50_16000 {ECO:0000313|EMBL:ATL49911.1};
OS Chitinophaga caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2029983 {ECO:0000313|EMBL:ATL49911.1, ECO:0000313|Proteomes:UP000220133};
RN [1] {ECO:0000313|EMBL:ATL49911.1, ECO:0000313|Proteomes:UP000220133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 {ECO:0000313|EMBL:ATL49911.1,
RC ECO:0000313|Proteomes:UP000220133};
RA Jin D., Kong X., Deng Y., Bai Z.;
RT "Paenichitinophaga pekingensis gen. nov., sp. nov., isolated from activated
RT sludge.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP023777; ATL49911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291R181; -.
DR KEGG; cbae:COR50_16000; -.
DR OrthoDB; 9760358at2; -.
DR Proteomes; UP000220133; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043214; F:ABC-type bacteriocin transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd18570; ABC_6TM_PCAT1_LagD_like; 1.
DR CDD; cd02418; Peptidase_C39B; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005897; Pept_C39_ABC_bacteriocin.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039421; Type_1_exporter.
DR NCBIfam; TIGR01193; bacteriocin_ABC; 1.
DR PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000220133};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..139
FT /note="Peptidase C39"
FT /evidence="ECO:0000259|PROSITE:PS50990"
FT DOMAIN 172..451
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 484..719
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 725 AA; 81295 MW; 63F5EEF9ED7A626F CRC64;
MWLNNRIKRK SKVKQRDLSD CGAACLSSIA AHYNLHIPVA RIRQYAYTDH KGTNVLGLIE
AAQKLGFEAK GVKGPFESLA KIPKPSIAHV VLKGVLHHYV VIYKVTKERI TIMDPADGKV
HEFKSEDFKK IWTGVLILIL PGENFKQEKL TSSHFQRFWY LLAPHKSILL QALFGSIVYT
ILGLSTSIYV QKIVDNVLVD GNKNLLNLLG SIMIVILLFQ LFIGNTKSIF ALKTGQQIDA
QLILGYYKHL LKLPQQFFDT MRVGEITSRI NDAVKIRSFI NDTAVGLVVN VFIVIFSFAV
MFAYYWKLAL IVLAIIPVYI VVYQLSNAFN KKLQRKLMED NAELGGQLVE SLNAASTIKR
FGLEEYANIK TENRFVKLLR TIFKSATTNL YIGSAASFVT SAFVVVILWI GSYFVIDRQL
TPGELLSFYA LLGYFTGPAM SLIGANKSMQ DALIASDRLF EILDLEQESN EQKMDLTPEM
LGDISFHNVS FKYNTRAEVF KDFNLHIRKG EITAIVGESG SGKSTLMNLL QNLYPLQAGQ
ICIGNIDIKY IHNDSLRKKI SVVPQHIDLF AGTVLENIAV GDFEADMQQV IKIAQVLGIM
EFIEKLPNGF LTLLGEHGVN LSGGQRQRLA IARAMYRNPD ILIFDEATSS LDPVSDQFVQ
LAVQQLKHAG KTIIIIAHRL STVMNADKIV VLHEGSMAEE GTHQQLLQKN SVYSKLWEHH
KGVII
//
