ID A0A158JGI6_9BURK Unreviewed; 698 AA.
AC A0A158JGI6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Peptidase family M50 {ECO:0000313|EMBL:SAL67966.1};
GN ORFNames=AWB65_06627 {ECO:0000313|EMBL:SAL67966.1};
OS Caballeronia humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326474 {ECO:0000313|EMBL:SAL67966.1, ECO:0000313|Proteomes:UP000054977};
RN [1] {ECO:0000313|EMBL:SAL67966.1, ECO:0000313|Proteomes:UP000054977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22934 {ECO:0000313|EMBL:SAL67966.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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DR EMBL; FCNW02000098; SAL67966.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158JGI6; -.
DR STRING; 326474.AWB65_06627; -.
DR OrthoDB; 9759690at2; -.
DR Proteomes; UP000054977; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR13325:SF3; MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE-2 PROTEASE; 1.
DR PANTHER; PTHR13325; PROTEASE M50 MEMBRANE-BOUND TRANSCRIPTION FACTOR SITE 2 PROTEASE; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 144..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 188..352
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 698 AA; 78990 MW; 536700B2C1B67FE9 CRC64;
MPVDPNLPSP ALRDDLRLGE ASNGRDGEPS WMIQDTVLNR FYRVGWLEFE CLARWEKPPA
QICKEINEET ALRPDLAQIL DFRRFLEQHE LLRPTPDALA RLRQRNRSGG WLTWRWWLHH
YLFFRIPLLR PQRFLTVVAR RLDWLFSPVT AIVVVLLSLA GIVLVLQQWD TFTGAVVESF
STEGLLSFAL ALAVAKTLHE LAHALVATRL GLRVAHMGIA FVVLWPMLYT DTGESWKLRS
SRQRLAIASA GILCELSLAG LATLGWALSD PGPLRNALLY LATTSWVLSL ALNASPFMRF
DGYFILSDLL DFPNLHQRAS ALARVSIRRT LLGLDDDWPE VFSTSHRRML VAFEFMTWIY
RLVLFLGIAV TVYLFFFKLL GAFLFVVEVT WFIAMPITRE LKHWWTQRSR IRPSRKLLLC
GIAGAFLLLV ALPWRTQIHA EGVARTERQL RVFVPFPARI QTIHPVGDVR ADDTLMVMDE
PDIASHMIGS EAGIRGYEAR LSGLIADAGG LDQQAATRER LRVQYEEARA AQSQIARLIL
RAPFAGKWMD VDPQWRAGQW INPKDQVGVL VDPGRWQVDA YVKQDDVQRL APGDAARFYP
TGQAVPIHGR VIAIDTTRAR ELAHPMLASR FKGPVAVTTE RDALTPNPPM FHVLVQLDGA
PPGLWETRGQ LQIDGNRRSW LIEGGTHLIA AFVRESGF
//
