ID V4PEV8_9CAUL Unreviewed; 1096 AA.
AC V4PEV8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN ORFNames=ABAC460_03075 {ECO:0000313|EMBL:ESQ92492.1};
OS Asticcacaulis sp. AC460.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282360 {ECO:0000313|EMBL:ESQ92492.1, ECO:0000313|Proteomes:UP000017839};
RN [1] {ECO:0000313|EMBL:ESQ92492.1, ECO:0000313|Proteomes:UP000017839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC460 {ECO:0000313|EMBL:ESQ92492.1,
RC ECO:0000313|Proteomes:UP000017839};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(2014).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
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:ESQ92492.1}.
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DR EMBL; AWGD01000006; ESQ92492.1; -; Genomic_DNA.
DR RefSeq; WP_023451984.1; NZ_AWGD01000006.1.
DR AlphaFoldDB; V4PEV8; -.
DR STRING; 1282360.ABAC460_03075; -.
DR PATRIC; fig|1282360.3.peg.606; -.
DR eggNOG; COG1404; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR OrthoDB; 5405281at2; -.
DR Proteomes; UP000017839; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 5.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR013858; Peptidase_M10B_C.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR42884:SF14; NEUROENDOCRINE CONVERTASE 1; 1.
DR PANTHER; PTHR42884; PROPROTEIN CONVERTASE SUBTILISIN/KEXIN-RELATED; 1.
DR Pfam; PF00353; HemolysinCabind; 5.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF08548; Peptidase_M10_C; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF51120; beta-Roll; 4.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 6.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 451..588
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT REGION 699..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1096 AA; 113115 MW; 42D5188D008D4D81 CRC64;
MLSKSGKIWL DERSSVALTA TTYTLPPAPA DDPSPVMQRP YGPAPLPVQM WSTGHEAQAE
SVATTAIFGT ISSATPTAGT GPRLGDDPLL YRQWYIDRTG LDNIGIDMNV RPVWDGGGGP
GYTGAGVTVG VFDSLIERNH PDLEANYNAG LDVDDLFYEH TDSAHGTAVA GIIAAVKNGI
GMTGIAYGAK VTSLPVIYTT SVSMHDFEIA MAHAKDFDVT NFSLGGLSPF DTGDTRLWFQ
LHGHYYKDAA ELGRDGLGTL LIQGAGNNRG INPLDANLSN FQNQRYSITV SATDSNGLVA
DYSSEGANVL VTAASSGAYY GPHIATTDQM GDAGYNKGDS PDWDPVSGDY TTRFGGTSAA
TPVISGIVAL VLEANPELGW RDVRDILAFS ARHAGVAFGG TPAWHEGYTW KVNHSSNVNG
TGLHYNQNYG FGLVDALAAV RLAESWTRQR TSANEVSRSD SVTQDLVIPE AQYNTTPLVV
EFEIAAGVTA QIVTLYMNMI HKMSNELQVK LISPSGTESL IFDHKGFGPS IYGTGGTAWA
PWTFTSNNFV GEDPAGTWRL EILDDRGFWP VNGVFKTATL TVYGDPTTDD SDYIYTNEFG
ALAGMDYGYT ITDTAGIDTL NAAAVTAASV LDLRGVAPAV INGKAVTIAA GTVIENAWGG
DGSDVLHGNG AANRLNGMRG NDTINGGLGD DTIDGGAGDD YVHGGAGNDE LSGGDGQDRL
SYEGATAGVT VDLSLSGVQD TGAGLDRLSG FETLQGSAWA DRLIGSGGDD VISAAGGHDT
VDGGAGNDTL SGGAGGDRLS GGAGIDRLSY GDSAAAVQVL LAANQASGGN AQGDVIDGFE
DVAGGAGNDT LVGDGGGNRL IGGNGGDALI GEAGNDTLEG GAGHDVLSGG DGDDRVSGGD
GNDMLGGRTG NDYVDGGLGN DTGFGGDGDD GLYGRDGNDN LSGELGRDTL DGGAGNDTLN
GGDGDDRLSG GLGADQLRGG NGNDVFIHRQ ADVVTTGDAH AVADMLMDFY PRAHHFQQYD
RIDLRAIDAI DGGTDDAFAL IGDAAFTAAG QLRVWFDGIN TRVEGNTIED GDGHVEFEII
LAGNLTALLG ATDFLL
//
