ID Q2CHH0_OCEGH Unreviewed; 717 AA.
AC Q2CHH0;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Peptidase, M50 family protein {ECO:0000313|EMBL:EAR52069.1};
GN ORFNames=OG2516_18430 {ECO:0000313|EMBL:EAR52069.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR52069.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR52069.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAR52069.1}.
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DR EMBL; AAOT01000006; EAR52069.1; -; Genomic_DNA.
DR RefSeq; WP_007256987.1; NZ_CH724110.1.
DR AlphaFoldDB; Q2CHH0; -.
DR STRING; 314256.OG2516_18430; -.
DR eggNOG; COG1994; Bacteria.
DR HOGENOM; CLU_019354_0_0_5; -.
DR OrthoDB; 9759690at2; -.
DR Proteomes; UP000003635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.10.1150; Coenzyme PQQ synthesis protein D (PqqD); 1.
DR InterPro; IPR001193; MBTPS2.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR041881; PqqD_sf.
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; PF13533; Biotin_lipoyl_2; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003635};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 158..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 465..510
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 504..556
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 717 AA; 78728 MW; 60308815C7001537 CRC64;
MAAGGSFHSD QWHRVAALRP RLRQHARIFR THYRGQLWYV LQDRTSGRFH RFTPESYFVL
SMFDGSRTLQ EVWDTSCAEL ESDALSQNEV ISLLGQLHGA DVLMGDLPPD IDEMAERGRK
MRRKKRVMSL MNPLAVRVPM FDPEGFLRVT APLVRPVLSW FGLLVWVAVV AYGVALAVVN
WEGLTTGIAD RVLSAESLVL LLLAYPVVKA LHELGHAYMI KRWGGEVHEI GLMFLVFMPV
PYIDASDSLS FQSKWQRAAV AGAGIMVEAM LAAIAVMVWD GAESGLVRAF AFNVILIGGV
STLFFNGNPL LRFDGYYVLS DLIEIPNLGR RANQYLGYLA QRYLLGVEEP KNPATAPGEP
AWFTFYAIAA FLYRLVIFSA IVLLVASRFF FVGVILAMWT VFLMFVLPML KHLWFVLTAP
QLRRRRGQAV ARVGAALAVV AGLLFVQPVP FSTLAEGVTL VPGSATIRPD ADGTVTGLAV
EQGQEVAAGD VLLTLEDPML DARVTLLEAT AAELRERAAT AAARDPNAAR IAREELAAAE
ADLALALERR DALTVRAGAA GQVVLAQPRD LAGRFVRQGE TLGYVTTFTD PLVRAVVPER
DADLVLKETK RMELRFASRP EEVLAARIVR EVPALSGTLP SRALATEGGG RVVLDPSSPS
GARALGNLLH LEVGVAPGTA FETIGERVHV RFVHEPASLA GRLYRRLRQV FLDQFDM
//
